Structure of PDB 1lbu Chain A

Receptor sequence
>1lbuA (length=213) Species: 1962 (Streptomyces albus G) [Search protein sequence]
DGCYTWSGTLSEGSSGEAVRQLQIRVAGYPGTGAQLAIDGQFGPATKAAV
QRFQSAYGLAADGIAGPATFNKIYQLQDDDCTPVNFTYAELNRCNSDWSG
GKVSAATARANALVTMWKLQAMRHAMGDKPITVNGGFRSVTCNSNVGGAS
NSRHMYGHAADLGAGSQGFCALAQAARNHGFTEILGPGYPGHNDHTHVAG
GDGRFWSAPSCGI
3D structure
PDB1lbu Structure of a Zn2+-Containing D-Alanyl-D-Alanine-Cleaving Carboxypeptidase at 2.5 A Resolution
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H154 D161 Y189 H192 D194 H195 H197
Catalytic site (residue number reindexed from 1) H154 D161 Y189 H192 D194 H195 H197
Enzyme Commision number 3.4.17.14: zinc D-Ala-D-Ala carboxypeptidase.
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 ZN A H154 D161 H197 H154 D161 H197
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0008237 metallopeptidase activity
GO:0009046 zinc D-Ala-D-Ala carboxypeptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0071555 cell wall organization
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:1lbu, PDBe:1lbu, PDBj:1lbu
PDBsum1lbu
PubMed
UniProtP00733|CBPM_STRAL Zinc D-Ala-D-Ala carboxypeptidase

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