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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
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN399
AASN410
AASN429
BASN399
BASN410
BASN429

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PDB entries from 2024-07-24

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