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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1bcr

E.C. namecarboxypeptidase D
SpeciesTriticum vulgare ()
E.C. Number (IntEnz) 3.4.16.6
CSA Homologues of 1bcrThere are 14 Homologs
CSA Entries With UniProtID P08819
CSA Entries With EC Number 3.4.16.6
PDBe Entry 1bcr
PDBSum Entry 1bcr
MACiE Entry M0005

Literature Report

IntroductionCarboxypeptidase D is a serine protease which specifically removes basic or hydrophobic residues from the C-terminus of the substrate protein.
Carboxypeptidase D is a member of the alpha beta hydrolase family and contains a Ser-His-Asp catalytic triad typical of the family. Carboxypeptidase D from yeast and wheat have had their structures determined, The wheat catalytic triad is made up of residues from both subunits of the homodimer whilst yeast carboxypeptidase D is a monomer, however, both have similar active site geometries.
MechansimCarboxypeptidase D uses a catalytic triad to activate serine 146 as a nucleophile to attack the scissile peptide bond. Histidine 397 and aspartate 338 from the neighbouring subunit complete the triad. The backbone amides of glycine 53 and tyrosine 147 make up the oxyanion hole to stabilise the tetrahedral intermediate.

Catalytic Sites for 1bcr

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GlyA5362macie:mainChainAmide
TyrA147159macie:mainChainAmide
SerA146158macie:sideChain
AspB338361macie:sideChain
HisB397413macie:sideChain

Literature References

Notes:
Bullock TL
Structure of the complex of L-benzylsuccinate with wheat serine carboxypeptidase II at 2.0-A resolution.
Biochemistry 1994 33 11127-11134
PubMed: 7727364
Bullock TL
Structure of the complex of L-benzylsuccinate with wheat serine carboxypeptidase II at 2.0-A resolution.
Biochemistry 1994 33 11127-11134
PubMed: 7727364
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