Structure of PDB 3q6v Chain B

Receptor sequence
>3q6vB (length=228) Species: 47917 (Serratia fonticola) [Search protein sequence]
NLTLTHFKGPLYIVEDKEYVQENSMVYIGTDGITIIGATWTPETAETLYK
EIRKVSPLPINEVINTNYHTDRAGGNAYWKTLGAKIVATQMTYDLQKSQW
GSIVNFTRQGNNKYPNLEKSLPDTVFPGDFNLQNGSIRAMYLGEAHTKDG
IFVYFPAERVLYGNCILKENLGNMSFANRTEYPKTLEKLKGLIEQGELKV
DSIIAGHDTPIHDVGLIDHYLTLLEKAP
3D structure
PDB3q6v Crystal structure of Serratia fonticola Sfh-I: activation of the nucleophile in mono-zinc metallo-beta-lactamases.
ChainB
Resolution1.37 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) N116 H118 D120 H196 C221 K224 N233 H263
Catalytic site (residue number reindexed from 1) N67 H69 D71 H146 C165 K168 N173 H207
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 GOL B H118 D120 H196 C221 N233 H263 H69 D71 H146 C165 N173 H207
BS02 ZN B D120 C221 H263 D71 C165 H207
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:3q6v, PDBe:3q6v, PDBj:3q6v
PDBsum3q6v
PubMed21762699
UniProtQ9RMI1

[Back to BioLiP]