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6Z6R

Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with manganese, N-oxalyl-alpha-methylalanine, and factor X substrate peptide fragment(39mer-4Ser)

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 Residues4
Detailsbinding site for residue MN A 801
ChainResidue
AHIS679
AHIS725
AUQK804
AHOH904

site_idAC2
Number of Residues4
Detailsbinding site for residue BR A 802
ChainResidue
ATYR371
APRO372
AGLN373
AASN639

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 803
ChainResidue
APHE450
APRO451
AASN452
ALYS420

site_idAC4
Number of Residues11
Detailsbinding site for residue UQK A 804
ChainResidue
ATRP625
ASER668
AMET670
AARG688
AHIS690
ATRP711
AHIS725
AARG735
AILE739
AMN801
AHOH904

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues33
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues33
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues32
DetailsRepeat: {"description":"TPR 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of human aspartate beta-hydroxylase isoform A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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