Structure of PDB 3d2z Chain A Binding Site BS02
Receptor Information
>3d2z Chain A (length=256) Species:
511145
(Escherichia coli str. K-12 substr. MG1655) [
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KGIVEKEGYQLDTRRQAQAAYPRIKVLVIHYTADDFDSSLATLTDKQVSS
HYLVPAVPPRYNGKPRIWQLVPEQELAWHAGISAWRGATRLNDTSIGIEL
ENRGWQKSAGVKYFAPFEPAQIQALIPLAKDIIARYHIKPENVVAHADIA
PQRKDDPGPLFPWQQLAQQGIGAWPDAQRVNFYLAGRAPHTPVDTASLLE
LLARYGYDVKPDMTPREQRRVIMAFQMHFRPTLYNGEADAETQAIAEALL
EKYGQD
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
3d2z Chain A Residue 262 [
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Receptor-Ligand Complex Structure
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PDB
3d2z
Specific Structural Features of the N-Acetylmuramoyl-l-Alanine Amidase AmiD from Escherichia coli and Mechanistic Implications for Enzymes of This Family.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
H35 H151 D161
Binding residue
(residue number reindexed from 1)
H30 H146 D156
Annotation score
4
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:3d2z
,
PDBe:3d2z
,
PDBj:3d2z
PDBsum
3d2z
PubMed
20036252
UniProt
P75820
|AMID_ECOLI N-acetylmuramoyl-L-alanine amidase AmiD (Gene Name=amiD)
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