Structure of PDB 2bh7 Chain A Binding Site BS01

Receptor Information
>2bh7 Chain A (length=254) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GIVEKEGYQLDTRRQAQAAYPRIKVLVIHYTADDFDSSLATLTDKQVSSH
YLVPAVPPRYNGKPRIWQLVPEQELAWHAGISAWRGATRLNDTSIGIELE
NRGWQKSAGVKYFAPFEPAQIQALIPLAKDIIARYHIKPENVVAHADIAP
QRKDDPGPLFPWQQLAQQGIGAWPDAQRVNFYLAGRAPHTPVDTASLLEL
LARYGYDVKPDMTPREQRRVIMAFQMHFRPTLYNGEADAETQAIAEALLE
KYGQ
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 chain2bh7 Chain A Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2bh7 Specific Structural Features of the N-Acetylmuramoyl-L-Alanine Amidase Amid from Escherichia Coli and Mechanistic Implications for Enzymes of This Family.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		H35 H151 D161
Binding residue
(residue number reindexed from 1)		H29 H145 D155
Annotation score4
Enzymatic activity
Enzyme Commision number 3.5.1.28: N-acetylmuramoyl-L-alanine amidase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008745 N-acetylmuramoyl-L-alanine amidase activity
GO:0009392 N-acetyl-anhydromuramoyl-L-alanine amidase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009253 peptidoglycan catabolic process
GO:0009254 peptidoglycan turnover
GO:0071555 cell wall organization
Cellular Component
GO:0009279 cell outer membrane
GO:0019867 outer membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2bh7, PDBe:2bh7, PDBj:2bh7
PDBsum2bh7
PubMed20036252
UniProtP75820|AMID_ECOLI N-acetylmuramoyl-L-alanine amidase AmiD (Gene Name=amiD)

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