Structure of PDB 2m5d Chain A

Receptor sequence
>2m5dA (length=227) Species: 1396 (Bacillus cereus) [Search protein sequence]
SQKVEKTVIKNETGTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSK
GLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKE
RGIKAHSTALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHT
EDNIVVWLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRY
RNINAVVPGHGEVGDKGLLLHTLDLLK
3D structure
PDB2m5d Solution structures of the Bacillus cereus metallo-beta-lactamase BcII and its complex with the broad spectrum inhibitor R-thiomandelic acid.
ChainA
ResolutionN/A
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) H86 H88 D90 H149 C168 K171 N180 H210
Catalytic site (residue number reindexed from 1) H86 H88 D90 H149 C168 K171 N180 H210
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 H86 H88 H149 H86 H88 H149
BS02 ZN A D90 H210 D90 H210
BS03 RTD A F34 W59 D90 H149 C168 H210 F34 W59 D90 H149 C168 H210
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:2m5d, PDBe:2m5d, PDBj:2m5d
PDBsum2m5d
PubMed24059435
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

[Back to BioLiP]