Structure of PDB 2y2d Chain B Binding Site BS01
Receptor Information
>2y2d Chain B (length=179) Species:
546
(Citrobacter freundii) [
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MLLDEGWLAEARRVPSPHYDCRPDDENPSLLVVHNISLPPGEFGGPWIDA
LFTGTIDPNAHPYFAGIAHLRVSAHCLIRRDGEIVQYVPFDKRAWHAGVS
SYQGRERCNDFSIGIELEGTDTLAYTDAQYQQLAAVTNALITRYPAIANN
MTGHCNIAPERKTDPGPSFDWARFRALVT
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
2y2d Chain B Residue 1180 [
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Receptor-Ligand Complex Structure
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PDB
2y2d
Crystal Structures of Bacterial Peptidoglycan Amidase Ampd and an Unprecedented Activation Mechanism.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
H34 H154 D164
Binding residue
(residue number reindexed from 1)
H34 H154 D164
Annotation score
4
Enzymatic activity
Enzyme Commision number
3.5.1.28
: N-acetylmuramoyl-L-alanine amidase.
Gene Ontology
Molecular Function
GO:0008745
N-acetylmuramoyl-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:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2y2d
,
PDBe:2y2d
,
PDBj:2y2d
PDBsum
2y2d
PubMed
21775432
UniProt
P82974
|AMPD_CITFR 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD (Gene Name=ampD)
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