Structure of PDB 1wup Chain D

Receptor sequence
>1wupD (length=217) Species: 615 (Serratia marcescens) [Search protein sequence]
SLPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFT
AKDTEKLVTWFVERGYKIKGSISSHFHSESTGGIEWLNSRSIPTYASELT
NELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERK
ILFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGD
ASLLKLTLEQAVKGLNE
3D structure
PDB1wup Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography.
ChainD
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H77 H79 E81 H139 C158 K161 N167 H197
Catalytic site (residue number reindexed from 1) H75 H77 E79 H137 C156 K159 N165 H195
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 ZN D H77 H79 E81 H139 H75 H77 E79 H137
BS02 ZN D E81 C158 H197 E79 C156 H195
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0042597 periplasmic space

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Cellular Component
External links
PDB RCSB:1wup, PDBe:1wup, PDBj:1wup
PDBsum1wup
PubMed15788415
UniProtP52699|BLAB_SERMA Metallo-beta-lactamase type 2

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