Structure of PDB 6bm9 Chain B Binding Site BS01

Receptor Information
>6bm9 Chain B (length=225) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EYPTASEIPDGEVRLYQIADGVWSHIAAQPLYPSNGLIVRDGDELLLIDT
AWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYA
SPSTRRLAKVEGTEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHSPDNLI
VYVPSARVLYGGCAIYELSRTSAGNVAAADLAEWPTSIERIQQHYPEAQF
VIPGHGLPGGLDLLKHTSDVVKAHT
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain6bm9 Chain B Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6bm9 Cryptic genetic variation shapes the adaptive evolutionary potential of enzymes.
Resolution2.19 Å
Binding residue
(original residue number in PDB)		H114 H116
Binding residue
(residue number reindexed from 1)		H79 H81
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H114 H116 D118 H179 C198 Y201 N210 H240
Catalytic site (residue number reindexed from 1) H79 H81 D83 H144 C163 Y166 N175 H205
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6bm9, PDBe:6bm9, PDBj:6bm9
PDBsum6bm9
PubMed30719972
UniProtQ5U7L7

[Back to BioLiP]