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6Q9I

Aspartyl/Asparaginyl beta-hydroxylase (AspH) H679A in complex with Factor X 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 Residues5
Detailsbinding site for residue FMT A 901
ChainResidue
ATRP625
ASER668
AARG735
AILE737
AHOH1170

site_idAC2
Number of Residues5
Detailsbinding site for residue FMT A 902
ChainResidue
AHOH1056
ALYS609
ASER626
AHIS671
AHOH1014

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 903
ChainResidue
AASP524
AGLY525
AHIS555
AHOH1140

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 904
ChainResidue
ASER455
AASN458
AASP459
AHOH1213

site_idAC5
Number of Residues5
Detailsbinding site for residue FMT B 201
ChainResidue
AARG393
AASN395
BGLU114
BGLY115
BPHE116

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

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AALA679
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

222415

PDB entries from 2024-07-10

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