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5APA

Crystal structure of human aspartate beta-hydroxylase isoform a

Replaces:  3RCQ
Functional Information from GO Data
ChainGOidnamespacecontents
A0018193biological_processpeptidyl-amino acid modification
A0042264biological_processpeptidyl-aspartic acid hydroxylation
A0062101molecular_functionpeptidyl-aspartic acid 3-dioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 1759
ChainResidue
AHIS679
AHIS725
ALMR1760
AHOH2056
AHOH2088

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE LMR A 1760
ChainResidue
AARG688
AHIS690
AHIS725
AARG735
AILE737
AILE739
ANI1759
AHOH2055
AHOH2056
ATRP625
ASER668
AMET670
AHIS679

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 1761
ChainResidue
ASER722

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.18
ChainResidueDetails
ATRP625
ASER668
AARG688
AARG735

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AHIS679
AHIS725

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN706

238268

PDB entries from 2025-07-02

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