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4KBZ

Crystal Structure of Hypoxia-Inducible Factor Prolyl Hydroxylase (PHD2) with (S)-{2-[2-(5-Cyano-3-hydroxy-pyridin-2-yl)-thiazol-4-yl]-acetylamino}-phenyl-acetic acid

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 Residues20
DetailsBINDING SITE FOR RESIDUE 1QA A 501
ChainResidue
AVAL241
AARG322
ATYR329
ALEU343
AHIS374
AVAL376
AARG383
ALYS408
AFE2502
AHOH624
AHOH625
ASER242
AHOH633
AARG252
ATRP258
AMET299
ATYR303
ATYR310
AHIS313
AASP315

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 502
ChainResidue
AHIS313
AASP315
AHIS374
A1QA501
AHOH624

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG396
AARG411
ALYS416

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
AHIS205
AARG370

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
AGLU357
AARG362
AHOH643

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

223532

PDB entries from 2024-08-07

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