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5AQ0

The structure of the Transthyretin-like domain of the first catalytic domain of the HUMAN Carboxypeptidase D

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006518biological_processpeptide metabolic process
A0008270molecular_functionzinc ion binding
B0004181molecular_functionmetallocarboxypeptidase activity
B0006518biological_processpeptide metabolic process
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 1464
ChainResidue
APHE419
BHIS462
AHOH2009
AHOH2010
AHOH2051
AHOH2053
BLEU434
BGLY436
BTYR437
BGLU449

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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