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3OUI

PHD2-R717 with 40787422

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0031418molecular_functionL-ascorbic acid binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 901
ChainResidue
AGLU357
AARG362

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 903
ChainResidue
AHOH46
AHOH109
ALYS332
AASP333
ALYS359

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 1
ChainResidue
AASP315
AHIS374
A42Z393
AHOH3
AHIS313

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 42Z A 393
ChainResidue
AFE21
AHOH3
AHOH17
AHOH20
AHOH30
AARG252
AMET299
ATYR310
AHIS313
AASP315
ATYR329
AHIS374
AVAL376
AARG383
APEG902

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 42Z A 2
ChainResidue
AHOH23
AVAL199
AASN203
AILE280
ACYS283
ALYS286
ASER289
ATYR290

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 902
ChainResidue
ALYS234
ATRP389
A42Z393

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16782814, ECO:0000269|PubMed:19604478, ECO:0000269|PubMed:28594552, ECO:0007744|PDB:2G19, ECO:0007744|PDB:3HQU, ECO:0007744|PDB:5V18
ChainResidueDetails
AHIS313
AASP315
AHIS374

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:19604478
ChainResidueDetails
AARG383

site_idSWS_FT_FI3
Number of Residues5
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:21601578
ChainResidueDetails
ACYS201
ACYS208
ACYS302
ACYS323
ACYS326

226707

PDB entries from 2024-10-30

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