Structure of PDB 6ogo Chain A Binding Site BS01

Receptor Information
>6ogo Chain A (length=229) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVD
TAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATY
ANALSNQLAPQKGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHT
SDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAF
PKASMIVMSHSAPDSRAAITHTARMADKL
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 chain6ogo Chain A 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]
PDB6ogo Flexible loops of New Delhi metallo-beta-lactamase modulate its activity towards different substrates.
Resolution1.43 Å
Binding residue
(original residue number in PDB)
H120 H122 H189
Binding residue
(residue number reindexed from 1)
H80 H82 H149
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H120 H122 D124 H189 C208 K211 N220 H250
Catalytic site (residue number reindexed from 1) H80 H82 D84 H149 C168 K171 N180 H210
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:6ogo, PDBe:6ogo, PDBj:6ogo
PDBsum6ogo
PubMed32353499
UniProtA0A1M2CSI6

[Back to BioLiP]