Structure of PDB 5ypk Chain A Binding Site BS03

Receptor Information
>5ypk Chain A (length=228) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTA
WTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYAN
ALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSD
NITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPK
ASMIVMSHSAPDSRAAITHTARMADKLR
Ligand information
Ligand IDHIW
InChIInChI=1S/C12H19N3O5S/c1-6(16)9(11(17)18)7-4-8(10(15-7)12(19)20)21-3-2-14-5-13/h5-9,16H,2-4H2,1H3,(H2,13,14)(H,17,18)(H,19,20)/t6-,7-,8+,9-/m1/s1
InChIKeyGGEWNUMDSNUHAH-LURQLKTLSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.4[H]/N=C\NCCS[C@H]1C[C@@H](N=C1C(=O)O)[C@@H]([C@@H](C)O)C(=O)O
OpenEye OEToolkits 2.0.4CC(C(C1CC(C(=N1)C(=O)O)SCCNC=N)C(=O)O)O
CACTVS 3.385C[C@@H](O)[C@H]([C@H]1C[C@H](SCCNC=N)C(=N1)C(O)=O)C(O)=O
CACTVS 3.385C[CH](O)[CH]([CH]1C[CH](SCCNC=N)C(=N1)C(O)=O)C(O)=O
ACDLabs 12.01O=C(O)C1=NC(CC1SCCN[C@H]=N)C(C(O)=O)C(O)C
FormulaC12 H19 N3 O5 S
Name(2R,4S)-2-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-[(2-{[(Z)-iminomethyl]amino}ethyl)sulfanyl]-3,4-dihydro-2H-pyrrole-5-ca rboxylic acid;
Hydrolyzed Imipenem
ChEMBL
DrugBank
ZINCZINC000139534184
PDB chain5ypk Chain A Residue 303 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5ypk The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		W93 H122 D124 H189 C208 K211 N220 H250
Binding residue
(residue number reindexed from 1)		W51 H80 D82 H147 C166 K169 N178 H208
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H120 H122 D124 H189 C208 K211 N220 H250
Catalytic site (residue number reindexed from 1) H78 H80 D82 H147 C166 K169 N178 H208
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5ypk, PDBe:5ypk, PDBj:5ypk
PDBsum5ypk
PubMed29269938
UniProtE5KIY2

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