Resource Cephalothin Group

Predicate	Value (sorted: none)
owl:sameAs	?:Gentamicin
ns1:interactsWith	?:Gentamicin
owl:sameAs	?:EXPT00891
owl:sameAs	?:Probenecid
ns1:interactsWith	?:Tobramycin
owl:sameAs	?:Tobramycin
ns1:description	" experimental This compound belongs to the 1,3-thiazines. These are organic compounds containing 1,3-thiazine, a six-member ring with a nitrogen and a sulfur atoms in ring positions 1 and 3 respectively, as well as two double bonds. 1,3-Thiazines Organic Compounds Heterocyclic Compounds Thiazines 1,3-Thiazines Dicarboxylic Acids and Derivatives Thiophenes Secondary Carboxylic Acid Amides Carboxylic Acid Esters Hemiaminals Enolates Ethers Enamines Polyamines Carboxylic Acids Thioethers Aminals Aldehydes thiophene hemiaminal carboxylic acid ester carboxamide group secondary carboxylic acid amide thioether aminal carboxylic acid derivative enolate ether enamine carboxylic acid polyamine organonitrogen compound amine aldehyde DB00798 Gentamicin Increased risk of nephrotoxicity DB00955 Netilmicin Increased risk of nephrotoxicity DB01032 Probenecid Probenecid may increase the serum level of cephalothin. DB00684 Tobramycin Increased risk of nephrotoxicity logP 0.77 ALOGPS logS -4.2 ALOGPS Water Solubility 2.79e-02 g/l ALOGPS logP 0.13 ChemAxon IUPAC Name (2R)-5-(2-methoxy-2-oxoethyl)-2-[(1R)-2-oxo-1-[2-(thiophen-2-yl)acetamido]ethyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid ChemAxon Traditional IUPAC Name (2R)-5-(2-methoxy-2-oxoethyl)-2-[(1R)-2-oxo-1-[2-(thiophen-2-yl)acetamido]ethyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid ChemAxon Molecular Weight 398.454 ChemAxon Monoisotopic Weight 398.060627698 ChemAxon SMILES [H][C@@](NC(=O)CC1=CC=CS1)(C=O)[C@]1([H])NC(C(O)=O)=C(CC(=O)OC)CS1 ChemAxon Molecular Formula C16H18N2O6S2 ChemAxon InChI InChI=1S/C16H18N2O6S2/c1-24-13(21)5-9-8-26-15(18-14(9)16(22)23)11(7-19)17-12(20)6-10-3-2-4-25-10/h2-4,7,11,15,18H,5-6,8H2,1H3,(H,17,20)(H,22,23)/t11-,15-/m1/s1 ChemAxon InChIKey InChIKey=UUWFGEKEQSCSMB-IAQYHMDHSA-N ChemAxon Polar Surface Area (PSA) 121.8 ChemAxon Refractivity 96.06 ChemAxon Polarizability 38.44 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 3.76 ChemAxon pKa (strongest basic) -2.5 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46936680 PubChem Substance 46506959 PDB CEP BE0001755 Beta-lactamase Toho-1 Escherichia coli # 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 Beta-lactamase Toho-1 Defense mechanisms and antibiotic degradation Has strong cefotaxime-hydrolyzing activity bla Cytoplasmic None 9.6 31447.0 Escherichia coli GenBank Gene Database D37830 GenBank Protein Database 1037162 UniProtKB Q47066 UniProt Accession BLT1_ECOLX Beta-lactamase Toho-1 precursor EC 3.5.2.6 >Beta-lactamase Toho-1 precursor MMTQSIRRSMLTVMATLPLLFSSATLHAQANSVQQQLEALEKSSGGRLGVALINTADNSQ ILYRADERFAMCSTSKVMAAAAVLKQSESDKHLLNQRVEIKKSDLVNYNPIAEKHVNGTM TLAELGAAALQYSDNTAMNKLIAHLGGPDKVTAFARSLGDETFRLDRTEPTLNTAIPGDP RDTTTPLAMAQTLKNLTLGKALAETQRAQLVTWLKGNTTGSASIRAGLPKSWVVGDKTGS GDYGTTNDIAVIWPENHAPLVLVTYFTQPEQKAERRRDILAAAAKIVTHGF >876 bp ATGATGACTCAGAGCATTCGCCGCTCAATGTTAACGGTGATGGCGACGCTACCCCTGCTA TTTAGCAGCGCAACGCTGCATGCGCAGGCGAACAGCGTGCAACAGCAGCTGGAAGCCCTG GAGAAAAGTTCGGGAGGTCGGCTTGGCGTTGCGCTGATTAACACCGCCGATAATTCGCAG ATTCTCTACCGTGCCGATGAACGTTTTGCGATGTGCAGTACCAGTAAGGTGATGGCGGCC GCGGCGGTGCTTAAACAGAGCGAGAGCGATAAGCACCTGCTAAATCAGCGCGTTGAAATC AAGAAGAGCGACCTGGTTAACTACAATCCCATTGCGGAGAAACACGTTAACGGCACGATG ACGCTGGCTGAGCTTGGCGCAGCGGCGCTGCAGTATAGCGACAATACTGCCATGAATAAG CTGATTGCCCATCTGGGTGGTCCCGATAAAGTGACGGCGTTTGCTCGCTCGTTGGGTGAT GAGACCTTCCGTCTGGACAGAACCGAGCCCACGCTCAATACCGCCATTCCAGGCGACCCG CGTGATACCACCACGCCGCTCGCGATGGCGCAGACCCTGAAAAATCTGACGCTGGGTAAA GCGCTGGCGGAAACTCAGCGGGCACAGTTGGTGACGTGGCTTAAGGGCAATACTACCGGT AGCGCGAGCATTCGGGCGGGTCTGCCGAAATCATGGGTAGTGGGCGATAAAACCGGCAGC GGAGATTATGGCACCACCAACGATATCGCGGTTATCTGGCCGGAAAACCACGCACCGCTG GTTCTGGTGACCTACTTTACCCAACCGGAGCAGAAGGCGGAAAGGCGTCGGGATATTCTG GCTGCGGCGGCGAAAATCGTAACCCACGGTTTCTGA PF00144 Beta-lactamase function beta-lactamase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function catalytic activity process metabolism process drug metabolism process cellular metabolism process antibiotic metabolism process antibiotic catabolism process beta-lactam antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process response to antibiotic process physiological process BE0001349 D-alanyl-D-alanine carboxypeptidase Streptomyces sp. (strain R61) # 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 D-alanyl-D-alanine carboxypeptidase Involved in cell wall peptidoglycan synthesis Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e., a D-alanyl-D-alanine- terminated peptide), it becomes immobilized in the form of a long- lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP) Secreted protein None 6.03 42917.0 Streptomyces sp. (strain R61) GenBank Gene Database X05109 GenBank Protein Database 515050 UniProtKB P15555 UniProt Accession DAC_STRSR D-alanyl-D-alanine carboxypeptidase precursor DD- peptidase DD-carboxypeptidase EC 3.4.16.4 >D-alanyl-D-alanine carboxypeptidase precursor MVSGTVGRGTALGAVLLALLAVPAQAGTAAAADLPAPDDTGLQAVLHTALSQGAPGAMVR VDDNGTIHQLSEGVADRATGRAITTTDRFRVGSVTKSFSAVVLLQLVDEGKLDLDASVNT YLPGLLPDDRITVRQVMSHRSGLYDYTNDMFAQTVPGFESVRNKVFSYQDLITLSLKHGV TNAPGAAYSYSNTNFVVAGMLIEKLTGHSVATEYQNRIFTPLNLTDTFYVHPDTVIPGTH ANGYLTPDEAGGALVDSTEQTVSWAQSAGAVISSTQDLDTFFSALMSGQLMSAAQLAQMQ QWTTVNSTQGYGLGLRRRDLSCGISVYGHTGTVQGYYTYAFASKDGKRSVTALANTSNNV NVLNTMARTLESAFCGKPTTAKLRSATSSATTVERHEDIAPGIARD >1221 bp ATGGTCTCAGGAACGGTGGGCAGAGGTACGGCGCTGGGCGCGGTGCTGTTGGCCCTCCTC GCAGTCCCCGCACAGGCCGGCACCGCCGCGGCCGCGGATCTGCCGGCACCCGACGACACC GGTCTGCAGGCGGTGCTGCACACGGCCCTTTCCCAGGGAGCCCCCGGTGCGATGGTGCGG GTCGACGACAACGGCACGATCCACCAGTTGTCGGAGGGAGTCGCCGACCGGGCCACCGGG CGTGCGATCACCACGACCGACCGGTTCCGCGTCGGCAGCGTCACCAAGAGCTTCTCCGCC GTGGTCCTGCTGCAACTGGTGGACGAGGGCAAGCTCGACCTGGACGCTTCGGTGAACACC TATCTGCCCGGGCTGCTGCCCGACGACCGGATCACCGTGCGTCAGGTGATGAGCCACCGC AGTGGGCTGTACGACTACACCAACGACATGTTCGCGCAGACGGTCCCGGGCTTCGAGTCC GTCCGCAACAAGGTCTTCAGCTACCAGGACCTGATCACCCTGTCCCTCAAGCACGGGGTC ACCAACGCACCGGGCGCGGCCTATTCATACTCCAACACGAACTTCGTCGTCGCGGGCATG CTCATCGAGAAGCTCACCGGCCACTCCGTGGCCACGGAGTACCAGAACCGCATCTTCACG CCGCTGAACCTGACCGACACCTTCTACGTGCACCCCGACACCGTCATCCCGGGCACCCAC GCCAACGGCTACCTCACGCCGGACGAGGCCGGTGGGGCCCTGGTCGACTCCACCGAGCAG ACGGTGTCGTGGGCGCAGAGCGCGGGCGCGGTCATCTCCAGCACGCAGGACCTGGACACG TTCTTCTCCGCGTTGATGAGCGGGCAGCTCATGTCCGCCGCGCAGCTCGCGCAGATGCAG CAGTGGACGACGGTCAACAGCACCCAGGGGTACGGCCTCGGCCTGCGCCGCCGTGACCTG TCCTGCGGTATCTCGGTGTACGGCCACACGGGCACCGTGCAGGGCTACTACACGTACGCC TTCGCCTCGAAGGACGGCAAGCGCAGCGTCACCGCGCTCGCCAACACCTCGAACAACGTG AACGTGCTGAACACGATGGCCCGCACGCTGGAATCCGCGTTCTGCGGCAAGCCGACGACC GCGAAGCTGCGCAGCGCGACCTCCTCGGCGACCACCGTGGAGCGCCACGAGGACATCGCG CCGGGTATCGCCCGCGACTGA PF00144 Beta-lactamase process response to chemical stimulus process response to drug process response to antibiotic process response to stimulus process response to abiotic stimulus "
rdfs:label	"Cephalothin Group"
ns1:interactsWith	?:Netilmicin
ns1:interactsWith	?:Probenecid
rdf:type	ns1:drugs
owl:sameAs	?:Netilmicin

" experimental This compound belongs to the 1,3-thiazines. These are organic compounds containing 1,3-thiazine, a six-member ring with a nitrogen and a sulfur atoms in ring positions 1 and 3 respectively, as well as two double bonds. 1,3-Thiazines Organic Compounds Heterocyclic Compounds Thiazines 1,3-Thiazines Dicarboxylic Acids and Derivatives Thiophenes Secondary Carboxylic Acid Amides Carboxylic Acid Esters Hemiaminals Enolates Ethers Enamines Polyamines Carboxylic Acids Thioethers Aminals Aldehydes thiophene hemiaminal carboxylic acid ester carboxamide group secondary carboxylic acid amide thioether aminal carboxylic acid derivative enolate ether enamine carboxylic acid polyamine organonitrogen compound amine aldehyde DB00798 Gentamicin Increased risk of nephrotoxicity DB00955 Netilmicin Increased risk of nephrotoxicity DB01032 Probenecid Probenecid may increase the serum level of cephalothin. DB00684 Tobramycin Increased risk of nephrotoxicity logP 0.77 ALOGPS logS -4.2 ALOGPS Water Solubility 2.79e-02 g/l ALOGPS logP 0.13 ChemAxon IUPAC Name (2R)-5-(2-methoxy-2-oxoethyl)-2-[(1R)-2-oxo-1-[2-(thiophen-2-yl)acetamido]ethyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid ChemAxon Traditional IUPAC Name (2R)-5-(2-methoxy-2-oxoethyl)-2-[(1R)-2-oxo-1-[2-(thiophen-2-yl)acetamido]ethyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid ChemAxon Molecular Weight 398.454 ChemAxon Monoisotopic Weight 398.060627698 ChemAxon SMILES [H][C@@](NC(=O)CC1=CC=CS1)(C=O)[C@]1([H])NC(C(O)=O)=C(CC(=O)OC)CS1 ChemAxon Molecular Formula C16H18N2O6S2 ChemAxon InChI InChI=1S/C16H18N2O6S2/c1-24-13(21)5-9-8-26-15(18-14(9)16(22)23)11(7-19)17-12(20)6-10-3-2-4-25-10/h2-4,7,11,15,18H,5-6,8H2,1H3,(H,17,20)(H,22,23)/t11-,15-/m1/s1 ChemAxon InChIKey InChIKey=UUWFGEKEQSCSMB-IAQYHMDHSA-N ChemAxon Polar Surface Area (PSA) 121.8 ChemAxon Refractivity 96.06 ChemAxon Polarizability 38.44 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 3.76 ChemAxon pKa (strongest basic) -2.5 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46936680 PubChem Substance 46506959 PDB CEP BE0001755 Beta-lactamase Toho-1 Escherichia coli # 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 Beta-lactamase Toho-1 Defense mechanisms and antibiotic degradation Has strong cefotaxime-hydrolyzing activity bla Cytoplasmic None 9.6 31447.0 Escherichia coli GenBank Gene Database D37830 GenBank Protein Database 1037162 UniProtKB Q47066 UniProt Accession BLT1_ECOLX Beta-lactamase Toho-1 precursor EC 3.5.2.6 >Beta-lactamase Toho-1 precursor MMTQSIRRSMLTVMATLPLLFSSATLHAQANSVQQQLEALEKSSGGRLGVALINTADNSQ ILYRADERFAMCSTSKVMAAAAVLKQSESDKHLLNQRVEIKKSDLVNYNPIAEKHVNGTM TLAELGAAALQYSDNTAMNKLIAHLGGPDKVTAFARSLGDETFRLDRTEPTLNTAIPGDP RDTTTPLAMAQTLKNLTLGKALAETQRAQLVTWLKGNTTGSASIRAGLPKSWVVGDKTGS GDYGTTNDIAVIWPENHAPLVLVTYFTQPEQKAERRRDILAAAAKIVTHGF >876 bp ATGATGACTCAGAGCATTCGCCGCTCAATGTTAACGGTGATGGCGACGCTACCCCTGCTA TTTAGCAGCGCAACGCTGCATGCGCAGGCGAACAGCGTGCAACAGCAGCTGGAAGCCCTG GAGAAAAGTTCGGGAGGTCGGCTTGGCGTTGCGCTGATTAACACCGCCGATAATTCGCAG ATTCTCTACCGTGCCGATGAACGTTTTGCGATGTGCAGTACCAGTAAGGTGATGGCGGCC GCGGCGGTGCTTAAACAGAGCGAGAGCGATAAGCACCTGCTAAATCAGCGCGTTGAAATC AAGAAGAGCGACCTGGTTAACTACAATCCCATTGCGGAGAAACACGTTAACGGCACGATG ACGCTGGCTGAGCTTGGCGCAGCGGCGCTGCAGTATAGCGACAATACTGCCATGAATAAG CTGATTGCCCATCTGGGTGGTCCCGATAAAGTGACGGCGTTTGCTCGCTCGTTGGGTGAT GAGACCTTCCGTCTGGACAGAACCGAGCCCACGCTCAATACCGCCATTCCAGGCGACCCG CGTGATACCACCACGCCGCTCGCGATGGCGCAGACCCTGAAAAATCTGACGCTGGGTAAA GCGCTGGCGGAAACTCAGCGGGCACAGTTGGTGACGTGGCTTAAGGGCAATACTACCGGT AGCGCGAGCATTCGGGCGGGTCTGCCGAAATCATGGGTAGTGGGCGATAAAACCGGCAGC GGAGATTATGGCACCACCAACGATATCGCGGTTATCTGGCCGGAAAACCACGCACCGCTG GTTCTGGTGACCTACTTTACCCAACCGGAGCAGAAGGCGGAAAGGCGTCGGGATATTCTG GCTGCGGCGGCGAAAATCGTAACCCACGGTTTCTGA PF00144 Beta-lactamase function beta-lactamase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function catalytic activity process metabolism process drug metabolism process cellular metabolism process antibiotic metabolism process antibiotic catabolism process beta-lactam antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process response to antibiotic process physiological process BE0001349 D-alanyl-D-alanine carboxypeptidase Streptomyces sp. (strain R61) # 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 D-alanyl-D-alanine carboxypeptidase Involved in cell wall peptidoglycan synthesis Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e., a D-alanyl-D-alanine- terminated peptide), it becomes immobilized in the form of a long- lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP) Secreted protein None 6.03 42917.0 Streptomyces sp. (strain R61) GenBank Gene Database X05109 GenBank Protein Database 515050 UniProtKB P15555 UniProt Accession DAC_STRSR D-alanyl-D-alanine carboxypeptidase precursor DD- peptidase DD-carboxypeptidase EC 3.4.16.4 >D-alanyl-D-alanine carboxypeptidase precursor MVSGTVGRGTALGAVLLALLAVPAQAGTAAAADLPAPDDTGLQAVLHTALSQGAPGAMVR VDDNGTIHQLSEGVADRATGRAITTTDRFRVGSVTKSFSAVVLLQLVDEGKLDLDASVNT YLPGLLPDDRITVRQVMSHRSGLYDYTNDMFAQTVPGFESVRNKVFSYQDLITLSLKHGV TNAPGAAYSYSNTNFVVAGMLIEKLTGHSVATEYQNRIFTPLNLTDTFYVHPDTVIPGTH ANGYLTPDEAGGALVDSTEQTVSWAQSAGAVISSTQDLDTFFSALMSGQLMSAAQLAQMQ QWTTVNSTQGYGLGLRRRDLSCGISVYGHTGTVQGYYTYAFASKDGKRSVTALANTSNNV NVLNTMARTLESAFCGKPTTAKLRSATSSATTVERHEDIAPGIARD >1221 bp ATGGTCTCAGGAACGGTGGGCAGAGGTACGGCGCTGGGCGCGGTGCTGTTGGCCCTCCTC GCAGTCCCCGCACAGGCCGGCACCGCCGCGGCCGCGGATCTGCCGGCACCCGACGACACC GGTCTGCAGGCGGTGCTGCACACGGCCCTTTCCCAGGGAGCCCCCGGTGCGATGGTGCGG GTCGACGACAACGGCACGATCCACCAGTTGTCGGAGGGAGTCGCCGACCGGGCCACCGGG CGTGCGATCACCACGACCGACCGGTTCCGCGTCGGCAGCGTCACCAAGAGCTTCTCCGCC GTGGTCCTGCTGCAACTGGTGGACGAGGGCAAGCTCGACCTGGACGCTTCGGTGAACACC TATCTGCCCGGGCTGCTGCCCGACGACCGGATCACCGTGCGTCAGGTGATGAGCCACCGC AGTGGGCTGTACGACTACACCAACGACATGTTCGCGCAGACGGTCCCGGGCTTCGAGTCC GTCCGCAACAAGGTCTTCAGCTACCAGGACCTGATCACCCTGTCCCTCAAGCACGGGGTC ACCAACGCACCGGGCGCGGCCTATTCATACTCCAACACGAACTTCGTCGTCGCGGGCATG CTCATCGAGAAGCTCACCGGCCACTCCGTGGCCACGGAGTACCAGAACCGCATCTTCACG CCGCTGAACCTGACCGACACCTTCTACGTGCACCCCGACACCGTCATCCCGGGCACCCAC GCCAACGGCTACCTCACGCCGGACGAGGCCGGTGGGGCCCTGGTCGACTCCACCGAGCAG ACGGTGTCGTGGGCGCAGAGCGCGGGCGCGGTCATCTCCAGCACGCAGGACCTGGACACG TTCTTCTCCGCGTTGATGAGCGGGCAGCTCATGTCCGCCGCGCAGCTCGCGCAGATGCAG CAGTGGACGACGGTCAACAGCACCCAGGGGTACGGCCTCGGCCTGCGCCGCCGTGACCTG TCCTGCGGTATCTCGGTGTACGGCCACACGGGCACCGTGCAGGGCTACTACACGTACGCC TTCGCCTCGAAGGACGGCAAGCGCAGCGTCACCGCGCTCGCCAACACCTCGAACAACGTG AACGTGCTGAACACGATGGCCCGCACGCTGGAATCCGCGTTCTGCGGCAAGCCGACGACC GCGAAGCTGCGCAGCGCGACCTCCTCGGCGACCACCGTGGAGCGCCACGAGGACATCGCG CCGGGTATCGCCCGCGACTGA PF00144 Beta-lactamase process response to chemical stimulus process response to drug process response to antibiotic process response to stimulus process response to abiotic stimulus "

ns1:interactsWith

?:Netilmicin

rdf:type

ns1:drugs

Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB03450"

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