Structure of PDB 6y6j Chain A

Receptor sequence

>6y6jA (length=231) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]

EYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELL
LIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGV
ATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHST
DNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYP
EAQFVIPGHGLPGGLDLLKHTTNVVKAHTNR

3D structure

PDB

6y6j Structure of metallo-beta-lactamase VIM-2 in complex with the imine and enamine form of hydrolysed Biapenem

Chain

Resolution

1.5 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)
BS01	OEN	A	F62 Y67 W87 H116 D118 H179 C198 R205 N210 H240 N261 R262	F31 Y36 W56 H85 D87 H148 C167 R174 N179 H209 N230 R231
BS02	OEQ	A	F62 Y67 W87 H116 D118 H179 C198 R205 N210 H240	F31 Y36 W56 H85 D87 H148 C167 R174 N179 H209
BS03	ZN	A	H114 H116 H179	H83 H85 H148
BS04	ZN	A	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

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:6y6j, PDBe:6y6j, PDBj:6y6j
PDBsum	6y6j
PubMed
UniProt	D1MEN9

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