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3ISQ

Crystal structure of human 4-Hydroxyphenylpyruvate dioxygenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0003868molecular_function4-hydroxyphenylpyruvate dioxygenase activity
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006559biological_processL-phenylalanine catabolic process
A0006572biological_processtyrosine catabolic process
A0009072biological_processaromatic amino acid metabolic process
A0016020cellular_componentmembrane
A0016701molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 901
ChainResidue
AHIS183
AHIS266
AGLU349
AHOH430
AHOH480

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
AHOH740
AHOH859
ANA902
AHIS218
AHOH438
AHOH444
AHOH479

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 902
ChainResidue
AHIS18
AGLU220
ACL401
AHOH436
AHOH438
AHOH445
AHOH479

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 910
ChainResidue
ATYR232
AGLN298
AHOH442
AEDO912

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 911
ChainResidue
ATYR221
ALYS270
AGLU272
ALYS369
AGLU372
AGLU373
AHOH443
AHOH470

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 912
ChainResidue
ATYR232
AGLU233
AGLN298
ALYS302
AEDO910

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 913
ChainResidue
ATRP122
APHE133
ATYR160
AHOH429
AHOH466
AHOH467
AHOH665

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AHIS183
AHIS266
AGLU349

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P49429
ChainResidueDetails
ALYS132

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER211

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49429
ChainResidueDetails
ASER226
ASER250

226707

PDB entries from 2024-10-30

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