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5JZU

Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, N-oxalylglycine and factor X substrate peptide fragment (26mer)

Functional Information from GO Data
ChainGOidnamespacecontents
A0018193biological_processpeptidyl-amino acid modification
A0042264biological_processpeptidyl-aspartic acid hydroxylation
A0062101molecular_functionpeptidyl-aspartic acid 3-dioxygenase activity
B0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MN A 801
ChainResidue
AHIS679
AHIS725
AOGA802
AHOH920
BASP103

site_idAC2
Number of Residues13
Detailsbinding site for residue OGA A 802
ChainResidue
AARG688
AHIS690
AHIS725
AARG735
AILE737
AILE739
AMN801
AHOH920
BASP103
ATRP625
ASER668
AMET670
AHIS679

Functional Information from PROSITE/UniProt
site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC
ChainResidueDetails
BASP86-CYS110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:6871167
ChainResidueDetails
AARG688
AARG735
BASP103
ASER668

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
ChainResidueDetails
AASN452

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN706

221051

PDB entries from 2024-06-12

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