Structure of PDB 6ewe Chain A

Receptor sequence
>6eweA (length=218) Species: 1396 (Bacillus cereus) [Search protein sequence]
KTVIKNETGTISISQLNKNVWVHTELGSAVPSNGLVLNTSKGLVLVDSSW
DDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTA
LTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLP
QYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPG
HGEVGDKGLLLHTLDLLK
3D structure
PDB6ewe Structure activity relationship studies on rhodanines and derived enethiol inhibitors of metallo-beta-lactamases.
ChainA
Resolution1.46 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) H77 H79 D81 H140 C159 K162 N171 H201
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 D81 C159 H201
BS02 ZN A H116 H118 H179 H77 H79 H140
BS03 C0W A H118 D120 H179 C198 N210 D213 H240 H79 D81 H140 C159 N171 D174 H201 MOAD: ic50=3.1uM
PDBbind-CN: -logKd/Ki=5.51,IC50=3.1uM
BindingDB: IC50=3100nM
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:6ewe, PDBe:6ewe, PDBj:6ewe
PDBsum6ewe
PubMed29655609
UniProtP04190|BLA2_BACCE Metallo-beta-lactamase type 2 (Gene Name=blm)

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