Structure of PDB 3wxc Chain B

Receptor sequence
>3wxcB (length=216) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
LPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTA
KDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELTN
ELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKI
LFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDA
SLLKLTLEQAVKGLNE
3D structure
PDB3wxc X-ray crystallographic analysis of IMP-1 metallo-beta-lactamase complexed with a 3-aminophthalic acid derivative, structure-based drug design, and synthesis of 3,6-disubstituted phthalic acid derivative inhibitors
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H77 H79 D81 H139 C158 K161 N167 H197
Catalytic site (residue number reindexed from 1) H74 H76 D78 H136 C155 K158 N164 H194
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 B H77 H79 H139 H74 H76 H136
BS02 ZN B D81 C158 H197 D78 C155 H194
BS03 C93 B V31 H79 S80 D81 H139 K161 G166 N167 H197 V28 H76 S77 D78 H136 K158 G163 N164 H194
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3wxc, PDBe:3wxc, PDBj:3wxc
PDBsum3wxc
PubMed25246278
UniProtQ79MP6

[Back to BioLiP]