Structure of PDB 3d2y Chain A Binding Site BS01
Receptor Information
>3d2y Chain A (length=257) Species:
511145
(Escherichia coli str. K-12 substr. MG1655) [
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EKGIVEKEGYQLDTRRQAQAAYPRIKVLVIHYTADDFDSSLATLTDKQVS
SHYLVPAVPPRYNGKPRIWQLVPEQELAWHAGISAWRGATRLNDTSIGIE
LENRGWQKSAGVKYFAPFEPAQIQALIPLAKDIIARYHIKPENVVAHADI
APQRKDDPGPLFPWQQLAQQGIGAWPDAQRVNFYLAGRAPHTPVDTASLL
ELLARYGYDVKPDMTPREQRRVIMAFQMHFRPTLYNGEADAETQAIAEAL
LEKYGQD
Ligand information
>3d2y Chain B (length=4) [
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gAEK
Receptor-Ligand Complex Structure
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PDB
3d2y
Specific Structural Features of the N-Acetylmuramoyl-l-Alanine Amidase AmiD from Escherichia coli and Mechanistic Implications for Enzymes of This Family.
Resolution
1.75 Å
Binding residue
(original residue number in PDB)
Y36 T37 V53 W83 H84 A85 G86 N97 E104 H151 R158 K159 D161
Binding residue
(residue number reindexed from 1)
Y32 T33 V49 W79 H80 A81 G82 N93 E100 H147 R154 K155 D157
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:3d2y
,
PDBe:3d2y
,
PDBj:3d2y
PDBsum
3d2y
PubMed
20036252
UniProt
P75820
|AMID_ECOLI N-acetylmuramoyl-L-alanine amidase AmiD (Gene Name=amiD)
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