Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB01955"
| Predicate | Value (sorted: default) |
|---|---|
| rdfs:label |
"1,4-Butanediol"
|
| rdf:type | |
| ns1:description |
"
110-63-4
experimental
# Satta R, Dimitrijevic N, Manev H: Drosophila metabolize 1,4-butanediol into gamma-hydroxybutyric acid in vivo. Eur J Pharmacol. 2003 Jul 25;473(2-3):149-52. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/12892832
# Zvosec DL, Smith SW, McCutcheon JR, Spillane J, Hall BJ, Peacock EA: Adverse events, including death, associated with the use of 1,4-butanediol. N Engl J Med. 2001 Jan 11;344(2):87-94. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11150358
# Poldrugo F, Snead OC 3rd: 1,4 Butanediol, gamma-hydroxybutyric acid and ethanol: relationships and interactions. Neuropharmacology. 1984 Jan;23(1):109-113. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/6717752
William E. Smith, "Production of tetrahydrofuran from 1,4-butanediol using tungsten on alumina catalysts." U.S. Patent US4136099, issued September, 1941.
This compound belongs to the polyamines. These are compounds containing more than one amine group.
Polyamines
Organic Compounds
Organonitrogen Compounds
Amines
Polyamines
Primary Alcohols
alcohol
logP
-0.63
ALOGPS
logS
0.87
ALOGPS
Water Solubility
6.75e+02 g/l
ALOGPS
logP
-0.63
ChemAxon
IUPAC Name
butane-1,4-diol
ChemAxon
Traditional IUPAC Name
1,4-butanediol
ChemAxon
Molecular Weight
90.121
ChemAxon
Monoisotopic Weight
90.068079564
ChemAxon
SMILES
OCCCCO
ChemAxon
Molecular Formula
C4H10O2
ChemAxon
InChI
InChI=1S/C4H10O2/c5-3-1-2-4-6/h5-6H,1-4H2
ChemAxon
InChIKey
InChIKey=WERYXYBDKMZEQL-UHFFFAOYSA-N
ChemAxon
Polar Surface Area (PSA)
40.46
ChemAxon
Refractivity
24.06
ChemAxon
Polarizability
10.16
ChemAxon
Rotatable Bond Count
3
ChemAxon
H Bond Acceptor Count
2
ChemAxon
H Bond Donor Count
2
ChemAxon
pKa (strongest acidic)
15.67
ChemAxon
pKa (strongest basic)
-2.4
ChemAxon
Physiological Charge
0
ChemAxon
Number of Rings
0
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
Water Solubility
1E+006 mg/L (at 20 °C)
YALKOWSKY,SH & DANNENFELSER,RM (1992)
Melting Point
20.1 °C
PhysProp
Boiling Point
235 °C
PhysProp
logP
-0.83
HANSCH,C ET AL. (1995)
pKa
14.5 (at 25 °C)
RIDDICK,JA ET AL. (1986)
ChEBI
41189
PubChem Compound
8064
PubChem Substance
46506248
Drugs Product Database (DPD)
2248224
ChemSpider
13835209
PDB
BU1
Wikipedia
1,4-Butanediol
BE0001414
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
Human
# Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284
# Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423
unknown
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
Involved in mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
Involved in the maturation of Asn-linked oligosaccharides. Trim a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). The only product is the Man(8)GlcNAc(2) isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. It may be involved in glycoprotein quality control since it is important to target misfolded glycoproteins for degradation
MAN1B1
9q34
Endoplasmic reticulum; endoplasmic reticulum membrane; single-pass type II membrane protein
85-105
7.8
79581.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:6823
GenAtlas
MAN1B1
GeneCards
MAN1B1
GenBank Gene Database
AF148509
GenBank Protein Database
6066222
UniProtKB
Q9UKM7
UniProt Accession
MA1B1_HUMAN
EC 3.2.1.113
ER alpha-1,2-mannosidase
Man9GlcNAc2-specific-processing alpha-mannosidase
Mannosidase alpha class 1B member 1
>Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
MAACEGRRSGALGSSQSDFLTPPVGGAPWAVATTVVMYPPPPPPPHRDFISVTLSFGENY
DNSKSWRRRSCWRKWKQLSRLQRNMILFLLAFLLFCGLLFYINLADHWKALAFRLEEEQK
MRPEIAGLKPANPPVLPAPQKADTDPENLPEISSQKTQRHIQRGPPHLQIRPPSQDLKDG
TQEEATKRQEAPVDPRPEGDPQRTVISWRGAVIEPEQGTELPSRRAEVPTKPPLPPARTQ
GTPVHLNYRQKGVIDVFLHAWKGYRKFAWGHDELKPVSRSFSEWFGLGLTLIDALDTMWI
LGLRKEFEEARKWVSKKLHFEKDVDVNLFESTIRILGGLLSAYHLSGDSLFLRKAEDFGN
RLMPAFRTPSKIPYSDVNIGTGVAHPPRWTSDSTVAEVTSIQLEFRELSRLTGDKKFQEA
VEKVTQHIHGLSGKKDGLVPMFINTHSGLFTHLGVFTLGARADSYYEYLLKQWIQGGKQE
TQLLEDYVEAIEGVRTHLLRHSEPSKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVYHG
LPASHMELAQELMETCYQMNRQMETGLSPEIVHFNLYPQPGRRDVEVKPADRHNLLRPET
VESLFYLYRVTGDRKYQDWGWEILQSFSRFTRVPSGGYSSINNVQDPQKPEPRDKMESFF
LGETLKYLFLLFSDDPNLLSLDAYVFNTEAHPLPIWTPA
>2100 bp
ATGGCTGCCTGCGAGGGCAGGAGAAGCGGAGCTCTCGGTTCCTCTCAGTCGGACTTCCTG
ACGCCGCCAGTGGGCGGGGCCCCTTGGGCCGTCGCCACCACTGTAGTCATGTACCCACCG
CCGCCGCCGCCGCCTCATCGGGACTTCATCTCGGTGACGCTGAGCTTTGGCGAGAGCTAT
GACAACAGCAAGAGTTGGCGGCGGCGCTCGTGCTGGAGGAAATGGAAGCAACTGTCGAGA
TTGCAGCGGAATATGATTCTCTTCCTCCTTGCCTTTCTGCTTTTCTGTGGACTCCTCTTC
TACATCAACTTGGCTGACCATTGGAAAGCTCTGGCTTTCAGGCTAGAGGAAGAGCAGAAG
ATGAGGCCAGAAATTGCTGGGTTAAAACCAGCAAATCCACCCGTCTTACCAGCTCCTCAG
AAGGCGGACACCGACCCTGAGAACTTACCTGAGATTTCGTCACAGAAGACACAAAGACAC
ATCCAGCGGGGACCACCTCACCTGCAGATTAGACCCCCAAGCCAAGACCTGAAGGATGGG
ACCCAGGAGGAGGCCACAAAAAGGCAAGAAGCCCCTGTGGATCCCCGCCCGGAAGGAGAT
CCGCAGAGGACAGTCATCAGCTGGAGGGGAGCGGTGATCGAGCCTGAGCAGGGCACCGAG
CTCCCTTCAAGAAGAGCAGAAGTGCCCACCAAGCCTCCCCTGCCACCGGCCAGGACACAG
GGCACACCAGTGCATCTGAACTATCGCCAGAAGGGCGTGATTGACGTCTTCCTGCATGCA
TGGAAAGGATACCGCAAGTTTGCATGGGGCCATGACGAGCTGAAGCCTGTGTCCAGGTCC
TTCAGTGAGTGGTTTGGCCTCGGTCTCACACTGATCGACGCGCTGGACACCATGTGGATC
TTGGGTCTGAGGAAAGAATTTGAGGAAGCCAGGAAGTGGGTGTCGAAGAAGTTACACTTT
GAAAAGGACGTGGACGTCAACCTGTTTGAGAGCACGATCCGCATCCTGGGGGGGCTCCTG
AGTGCCTACCACCTGTCTGGGGACAGCCTCTTCCTGAGGAAAGCTGAGGATTTTGGAAAT
CGGCTAATGCCTGCCTTCAGAACACCATCCAAGATTCCTTACTCGGATGTGAACATCGGT
ACTGGAGTTGCCCACCCGCCACGGTGGACCTCCGACAGCACTGTGGCCGAGGTGACCAGC
ATTCAGCTGGAGTTCCGGGAGCTCTCCCGTCTCACAGGGGATAAGAAGTTTCAGGAGGCA
GTGGAGAAGGTGACACAGCACATCCACGGCCTGTCTGGGAAGAAGGATGGGCTGGTGCCC
ATGTTCATCAATACCCACAGTGGCCTCTTCACCCACCTGGGCGTATTCACGCTGGGCGCC
AGGGCCGACAGCTACTATGAGTACCTGCTGAAGCAGTGGATCCAGGGCGGGAAGCAGGAG
ACACAGCTGCTGGAAGACTACGTGGAAGCCATCGAGGGTGTCAGAACGCACCTGCTGCGG
CACTCCGAGCCCAGTAAGCTCACCTTTGTGGGGGAGCTTGCCCACGGCCGCTTCAGTGCC
AAGATGGACCACCTGGTGTGCTTCCTGCCAGGGACGCTGGCTCTGGGCGTCTACCACGGC
CTGCCCGCCAGCCACATGGAGCTGGCCCAGGAGCTCATGGAGACTTGTTACCAGATGAAC
CGGCAGATGGAGACGGGGCTGAGTCCCGAGATCGTGCACTTCAACCTTTACCCCCAGCCG
GGCCGTCGGGACGTGGAGGTCAAGCCAGCAGACAGGCACAACCTGCTGCGGCCAGAGACC
GTGGAGAGCCTGTTCTACCTGTACCGCGTCACAGGGGACCGCAAATACCAGGACTGGGGC
TGGGAGATTCTGCAGAGCTTCAGCCGATTCACACGGGTCCCCTCGGGTGGCTATTCTTCC
ATCAACAATGTCCAGGATCCTCAGAAGCCCGAGCCTAGGGACAAGATGGAGAGCTTCTTC
CTGGGGGAGACGCTCAAGTATCTGTTCTTGCTCTTCTCCGATGACCCAAACCTGCTCAGC
CTGGACGCCTACGTGTTCAACACCGAAGCCCACCCTCTGCCTATCTGGACCCCTGCCTAG
PF01532
Glyco_hydro_47
component
cell
component
membrane
function
catalytic activity
function
calcium ion binding
function
hydrolase activity, acting on glycosyl bonds
function
hydrolase activity
function
hydrolase activity, hydrolyzing O-glycosyl compounds
function
mannosidase activity
function
mannosyl-oligosaccharide mannosidase activity
function
mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
function
ion binding
function
cation binding
function
binding
process
metabolism
process
macromolecule metabolism
process
biopolymer metabolism
process
biopolymer modification
process
protein modification
process
protein amino acid glycosylation
process
protein amino acid N-linked glycosylation
process
physiological process
BE0001640
Phospholipase A2, membrane associated
Human
# Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284
# Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423
# Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
Phospholipase A2, membrane associated
Involved in phospholipase A2 activity
Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
PLA2G2A
1p35
Membrane; peripheral membrane protein
None
9.51
16083.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9031
GenAtlas
PLA2G2A
GeneCards
PLA2G2A
GenBank Gene Database
M22430
GenBank Protein Database
190889
UniProtKB
P14555
UniProt Accession
PA2GA_HUMAN
EC 3.1.1.4
GIIC sPLA2
Group IIA phospholipase A2
Non-pancreatic secretory phospholipase A2
NPS-PLA2
Phosphatidylcholine 2-acylhydrolase
Phospholipase A2, membrane associated precursor
>Phospholipase A2, membrane associated precursor
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
>435 bp
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
PF00068
Phospholip_A2_1
function
ion binding
function
cation binding
function
calcium ion binding
function
hydrolase activity, acting on ester bonds
function
binding
function
carboxylic ester hydrolase activity
function
lipase activity
function
catalytic activity
function
phospholipase activity
function
phospholipase A2 activity
function
hydrolase activity
process
primary metabolism
process
lipid metabolism
process
physiological process
process
metabolism
process
lipid catabolism
BE0003768
Group IIE secretory phospholipase A2
Human
# Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284
# Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423
# Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
Group IIE secretory phospholipase A2
Involved in calcium ion binding
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids
PLA2G2E
1p36.13
Secreted
None
8.28
15988.5
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:13414
GeneCards
PLA2G2E
GenBank Gene Database
AF189279
GenBank Protein Database
7108923
UniProtKB
Q9NZK7
UniProt Accession
PA2GE_HUMAN
GIIE sPLA2
Phosphatidylcholine 2-acylhydrolase GIIE
sPLA(2)-IIE
>Group IIE secretory phospholipase A2
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
PF00068
Phospholip_A2_1
function
lipase activity
function
catalytic activity
function
phospholipase activity
function
phospholipase A2 activity
function
hydrolase activity
function
ion binding
function
cation binding
function
calcium ion binding
function
hydrolase activity, acting on ester bonds
function
binding
function
carboxylic ester hydrolase activity
process
metabolism
process
lipid catabolism
process
primary metabolism
process
lipid metabolism
process
physiological process
BE0001276
Ribosomal small subunit pseudouridine synthase A
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
# Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284
# Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423
unknown
Ribosomal small subunit pseudouridine synthase A
Translation, ribosomal structure and biogenesis
Responsible for synthesis of pseudouridine from uracil- 516 in 16S ribosomal RNA
rsuA
Cytoplasmic
None
4.75
26213.0
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
GenBank Gene Database
L42023
GenBank Protein Database
1574175
UniProtKB
P45124
UniProt Accession
RSUA_HAEIN
16S pseudouridine 516 synthase
16S pseudouridylate 516 synthase
EC 5.4.99.-
rRNA pseudouridylate synthase A
rRNA- uridine isomerase A
>Ribosomal small subunit pseudouridine synthase A
MRLDKFIAENVGLTRSQATKAIRQSAVKINGEIVKSGSVQISQEDEIYFEDELLTWIEEG
QYFMLNKPQGCVCSNDDGDYPTIYQFFDYPLAGKLHSAGRLDVDTTGLVLLTDDGQWSHR
ITSPKHHCEKTYLVTLADPVEENYSAACAEGILLRGEKEPTKPAKLEILDDYNVNLTISE
GRYHQVKRMFAALGNKVVGLHRWKIGDVVLDESLEEGEYRPLTQSEIEKLVK
>699 bp
TTATTTTACTAACTTTTCAATTTCACTTTGAGTTAATGGGCGGTATTCGCCTTCTTCTAA
GGATTCATCCAACACTACATCACCAATTTTCCAGCGATGTAATCCAACGACTTTATTCCC
AAGTGCGGCAAACATACGTTTTACTTGATGATAACGACCTTCAGAAATGGTCAGATTCAC
ATTGTAGTCATCTAAAATTTCTAATTTTGCTGGTTTAGTGGGCTCTTTTTCTCCGCGTAA
TAAAATGCCTTCTGCACAAGCTGCTGAATAATTTTCTTCTACGGGATCAGCTAATGTCAC
CAAATAGGTTTTTTCACAATGATGCTTTGGGGAAGTGATGCGATGTGACCATTGTCCATC
ATCGGTAAGCAATACGAGACCTGTCGTATCCACATCTAAGCGACCTGCGCTATGTAATTT
TCCAGCTAAAGGGTAATCAAAAAATTGATAAATTGTTGGATAGTCGCCGTCATCATTAGA
ACAAACACAGCCTTGTGGTTTATTCAACATAAAATACTGGCCTTCTTCGATCCAAGTTAA
TAATTCATCTTCAAAATAAATTTCGTCTTCTTGTGAAATTTGAACCGAACCACTTTTGAC
AATTTCACCGTTGATTTTTACCGCACTTTGGCGGATCGCTTTTGTTGCTTGAGAACGAGT
TAATCCCACATTTTCAGCAATAAATTTATCTAATCTCAT
PF01479
S4
PF00849
PseudoU_synth_2
function
catalytic activity
function
intramolecular transferase activity
function
pseudouridylate synthase activity
function
pseudouridine synthase activity
function
lyase activity
function
nucleic acid binding
function
RNA binding
function
isomerase activity
function
binding
function
carbon-oxygen lyase activity
function
hydro-lyase activity
process
metabolism
process
cellular metabolism
process
RNA processing
process
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
process
RNA metabolism
process
physiological process
BE0002005
Penicillin-insensitive murein endopeptidase
Escherichia coli (strain K12)
# Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284
# Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423
unknown
Penicillin-insensitive murein endopeptidase
Cell wall/membrane/envelope biogenesis
Involved in the removal of murein from the sacculus. May also facilitate integration of nascent murein strands into the sacculus by cleaving the peptide bonds between neighboring strands in mature murein
mepA
Periplasm
None
8.4
30137.0
Escherichia coli (strain K12)
GenBank Gene Database
X16909
GenBank Protein Database
41993
UniProtKB
P0C0T5
UniProt Accession
MEPA_ECOLI
D-alanyl-D-alanine-endopeptidase
DD-endopeptidase
EC 3.4.24.-
>Penicillin-insensitive murein endopeptidase precursor
MNKTAIALLALLASSASLAATPWQKITQPVPGSAQSIGSFSNGCIVGADTLPIQSEHYQV
MRTDQRRYFGHPDLVMFIQRLSSQVSNLGMGTVLIGDMGMPAGGRFNGGHASHQTGLDVD
IFLQLPKTRWTSAQLLRPQALDLVSRDGKHVVSTLWKPEIFSLIKLAAQDKDVTRIFVNP
AIKQQLCLDAGTDRDWLRKVRPWFQHRAHMHVRLRCPADSLECEDQPLPPSGDGCGAELQ
SWFEPPKPGTTKPEKKTPPPLPPSCQALLDEHVI
>825 bp
ATGAATAAAACCGCGATTGCGCTGCTGGCTCTGCTTGCCAGTAGCGCCAGCCTGGCAGCG
ACGCCGTGGCAAAAAATAACCCAACCTGTGCCGGGTAGCGCACAATCGATAGGCAGTTTT
TCTAATGGCTGTATTGTCGGCGCTGACACGCTGCCGATACAGTCCGAACATTATCAGGTC
ATGCGTACCGATCAGCGTCGCTATTTCGGTCACCCGGATCTGGTGATGTTTATCCAGCGT
CTGAGTAGCCAGGTGAGCAATCTGGGCATGGGTACGGTGCTGATTGGCGATATGGGGATG
CCCGCTGGTGGGCGTTTCAACGGCGGTCATGCCAGCCACCAGACCGGACTGGATGTCGAT
ATCTTTCTGCAACTGCCGAAAACTCGCTGGACCTCCGCGCAGCTCTTGCGCCCGCAAGCA
CTGGACTTAGTTTCCCGCGACGGTAAACACGTTGTCTCCACGCTGTGGAAGCCAGAAATT
TTCAGCTTGATCAAACTCGCCGCCCAGGACAAAGACGTCACGCGCATTTTTGTTAATCCG
GCGATTAAACAACAACTTTGCCTTGATGCGGGCACCGATCGCGACTGGTTGCGCAAAGTG
CGACCCTGGTTCCAGCATCGCGCGCATATGCATGTACGATTACGTTGCCCTGCCGATAGT
CTGGAGTGTGAAGATCAACCTTTACCGCCATCAGGCGATGGTTGCGGGGCAGAACTGCAA
AGCTGGTTTGAACCTCCAAAACCGGGAACAACAAAGCCTGAGAAGAAGACACCGCCTCCG
TTGCCGCCTTCCTGCCAGGCGCTACTGGATGAGCACGTGATCTAA
PF03411
Peptidase_M74
component
periplasmic space
component
periplasmic space (sensu Gram-negative Bacteria)
component
cell
function
peptidase activity
function
endopeptidase activity
function
serine-type endopeptidase activity
function
catalytic activity
function
hydrolase activity
function
murein DD-endopeptidase activity
process
protein metabolism
process
cellular protein metabolism
process
physiological process
process
proteolysis
process
metabolism
process
macromolecule metabolism
"
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| owl:sameAs |
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines/drugbank_small.nt
The resource does not appear as an object