Structure of PDB 5fqb Chain A

Receptor sequence
>5fqbA (length=219) Species: 1396 (Bacillus cereus) [Search protein sequence]
KTVIKNETGTISISQLNKNVWVHTELGSFAVPSNGLVLNTSKGLVLVDSS
WDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHST
ALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWL
PQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVP
GHGEVGDKGLLLHTLDLLK
3D structure
PDB5fqb Structural basis of metallo-beta-lactamase, serine-beta-lactamase and penicillin-binding protein inhibition by cyclic boronates.
ChainA
Resolution1.899 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H119 H121 D123 H199 C224 K227 N236 H266
Catalytic site (residue number reindexed from 1) H78 H80 D82 H141 C160 K163 N172 H202
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 C224 H266 C160 H202
BS02 ZN A H119 H121 H199 H78 H80 H141
BS03 OK3 A F65 W90 H119 H121 A122 D123 H199 C224 N236 D239 H266 F29 W51 H78 H80 A81 D82 H141 C160 N172 D175 H202 MOAD: ic50=0.3uM
PDBbind-CN: -logKd/Ki=6.52,IC50=0.3uM
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:5fqb, PDBe:5fqb, PDBj:5fqb
PDBsum5fqb
PubMed27499424
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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