Structure of PDB 3d2y Chain A

Receptor sequence
>3d2yA (length=257) Species: 511145 (Escherichia coli str. K-12 substr. MG1655) [Search protein sequence]
EKGIVEKEGYQLDTRRQAQAAYPRIKVLVIHYTADDFDSSLATLTDKQVS
SHYLVPAVPPRYNGKPRIWQLVPEQELAWHAGISAWRGATRLNDTSIGIE
LENRGWQKSAGVKYFAPFEPAQIQALIPLAKDIIARYHIKPENVVAHADI
APQRKDDPGPLFPWQQLAQQGIGAWPDAQRVNFYLAGRAPHTPVDTASLL
ELLARYGYDVKPDMTPREQRRVIMAFQMHFRPTLYNGEADAETQAIAEAL
LEKYGQD
3D structure
PDB3d2y Specific Structural Features of the N-Acetylmuramoyl-l-Alanine Amidase AmiD from Escherichia coli and Mechanistic Implications for Enzymes of This Family.
ChainA
Resolution1.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.28: N-acetylmuramoyl-L-alanine amidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide A Y36 T37 V53 W83 H84 A85 G86 N97 E104 H151 R158 K159 D161 Y32 T33 V49 W79 H80 A81 G82 N93 E100 H147 R154 K155 D157
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
PDBsum3d2y
PubMed20036252
UniProtP75820|AMID_ECOLI N-acetylmuramoyl-L-alanine amidase AmiD (Gene Name=amiD)

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