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5JTC

Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, 2,4-pyridine dicarboxylate 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 Residues5
Detailsbinding site for residue MN A 801
ChainResidue
AHIS679
AHIS725
APD2802
BASP103
BHOH203

site_idAC2
Number of Residues15
Detailsbinding site for residue PD2 A 802
ChainResidue
AARG688
AHIS690
AHIS725
AVAL727
AARG735
AILE737
AMN801
AHOH909
BASP103
BHOH203
BHOH206
ATRP625
ASER668
AMET670
AHIS679

site_idAC3
Number of Residues4
Detailsbinding site for residue BR A 803
ChainResidue
ATYR371
APRO372
AGLN373
AASN639

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 804
ChainResidue
ALYS420
APHE450
APRO451
AASN452
AASP453

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
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

224931

PDB entries from 2024-09-11

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