Structure of PDB 3d2z Chain A

Receptor sequence
>3d2zA (length=256) Species: 511145 (Escherichia coli str. K-12 substr. MG1655) [Search protein sequence]
KGIVEKEGYQLDTRRQAQAAYPRIKVLVIHYTADDFDSSLATLTDKQVSS
HYLVPAVPPRYNGKPRIWQLVPEQELAWHAGISAWRGATRLNDTSIGIEL
ENRGWQKSAGVKYFAPFEPAQIQALIPLAKDIIARYHIKPENVVAHADIA
PQRKDDPGPLFPWQQLAQQGIGAWPDAQRVNFYLAGRAPHTPVDTASLLE
LLARYGYDVKPDMTPREQRRVIMAFQMHFRPTLYNGEADAETQAIAEALL
EKYGQD
3D structure
PDB3d2z Specific Structural Features of the N-Acetylmuramoyl-l-Alanine Amidase AmiD from Escherichia coli and Mechanistic Implications for Enzymes of This Family.
ChainA
Resolution2.8 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 V53 W83 H84 G86 N97 E104 H151 R158 V48 W78 H79 G81 N92 E99 H146 R153
BS02 ZN A H35 H151 D161 H30 H146 D156
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
PDBsum3d2z
PubMed20036252
UniProtP75820|AMID_ECOLI N-acetylmuramoyl-L-alanine amidase AmiD (Gene Name=amiD)

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