Structure of PDB 4c1e Chain B

Receptor sequence
>4c1eB (length=231) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
EYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELL
LIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGV
ATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHST
DNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYP
EAQFVIPGHGLPGGLDLLKHTTNVVKAHTNR
3D structure
PDB4c1e Structural Basis of Metallo-beta-Lactamase Inhibition by Captopril Stereoisomers.
ChainB
Resolution1.399 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H114 H116 D118 H179 C198 Y201 N210 H240
Catalytic site (residue number reindexed from 1) H83 H85 D87 H148 C167 Y170 N179 H209
Enzyme Commision number 3.5.2.6: beta-lactamase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MCO B F62 Y67 W87 H116 D118 H179 R205 G209 N210 H240 F31 Y36 W56 H85 D87 H148 R174 G178 N179 H209
BS02 ZN B H114 H116 H179 H83 H85 H148
BS03 ZN B D118 C198 H240 D87 C167 H209
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4c1e, PDBe:4c1e, PDBj:4c1e
PDBsum4c1e
PubMed26482303
UniProtQ9K2N0

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