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5JZA

Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese and N-oxalylglycine

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
AOGA806
AHOH939
AHOH1005

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 802
ChainResidue
AHOH931
ASER455
AASN458
AASP459
APRO520

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 803
ChainResidue
ATYR544
ATRP560
AGOL804

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL A 804
ChainResidue
ATRP560
AASN706
AGOL803

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL A 805
ChainResidue
ALEU466
AARG526

site_idAC6
Number of Residues11
Detailsbinding site for residue OGA A 806
ChainResidue
ATRP625
ASER668
AMET670
AHIS679
AARG688
AHIS690
AHIS725
AVAL727
AARG735
AILE739
AMN801

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
ChainResidueDetails
AASN452

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

218853

PDB entries from 2024-04-24

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