Structure of PDB 6f2n Chain A

Receptor sequence
>6f2nA (length=219) Species: 1396 (Bacillus cereus) [Search protein sequence]
EKTVIKNETGTISISQLNKNVWVHTELGSAVPSNGLVLNTSKGLVLVDSS
WDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHST
ALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWL
PQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVP
GHGEVGDKGLLLHTLDLLK
3D structure
PDB6f2n Structure activity relationship studies on rhodanines and derived enethiol inhibitors of metallo-beta-lactamases.
ChainA
Resolution1.149 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H116 H118 D120 H179 C198 K201 N210 H240
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 D120 C198 H240 D82 C160 H202
BS02 ZN A H116 H118 H179 H78 H80 H141
BS03 CF8 A V69 H118 D120 H179 C198 N210 H240 V31 H80 D82 H141 C160 N172 H202 MOAD: ic50=0.2uM
PDBbind-CN: -logKd/Ki=6.70,IC50=0.2uM
BindingDB: IC50=200nM
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:6f2n, PDBe:6f2n, PDBj:6f2n
PDBsum6f2n
PubMed29655609
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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