Structure of PDB 2qds Chain A

Receptor sequence
>2qdsA (length=224) Species: 644 (Aeromonas hydrophila) [Search protein sequence]
AGMSLTQVSGPVYVVEDNYYVQENSMVYFGAKGVTVVGATWTPDTARELH
KLIKRVSRKPVLEVINTNYHTDRAGGNAYWKSIGAKVVSTRQTRDLMKSD
WAEIVAFTRKGLPEYPDLPLVLPNVVHDGDFTLQEGKVRAFYAGPAHTPD
GIFVYFPDEQVLYGNCILKEKLGNLSFADVKAYPQTLERLKAMKLPIKTV
IGGHDSPLHGPELIDHYEALIKAA
3D structure
PDB2qds Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols.
ChainA
Resolution1.66 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N116 H118 D120 H196 C221 K224 N233 H263
Catalytic site (residue number reindexed from 1) N68 H70 D72 H147 C166 K169 N174 H204
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 A D120 C221 H263 A304 D72 C166 H204 A224
BS02 MCO A D120 H196 N233 D72 H147 N174 MOAD: Ki=72uM
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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Molecular Function
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Cellular Component
External links
PDB RCSB:2qds, PDBe:2qds, PDBj:2qds
PDBsum2qds
PubMed18563261
UniProtP26918|BLAB_AERHY Metallo-beta-lactamase type 2 (Gene Name=cphA)

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