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6QGV

HIF prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with a Spiro[4.5]decanone inhibitor (JPHM-2-167)

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 Residues5
Detailsbinding site for residue MN A 501
ChainResidue
AHIS313
AASP315
AHIS374
AJ2H502
AHOH626

site_idAC2
Number of Residues17
Detailsbinding site for residue J2H A 502
ChainResidue
AASP315
AASP320
AARG322
AHIS374
AVAL376
ATRP389
ALYS402
ATYR403
AMN501
AHOH626
AHOH686
AHOH707
AHOH715
ATRP258
ATHR296
ATYR303
AHIS313

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 503
ChainResidue
ALYS350
AALA351
AGLN352
AHOH605
AHOH703
AHOH716

site_idAC4
Number of Residues4
Detailsbinding site for residue IPA A 504
ChainResidue
AASP277
AARG281
AASN293
AGLY294

site_idAC5
Number of Residues12
Detailsbinding site for residue SO4 A 505
ChainResidue
APRO264
APRO264
AGLY265
AGLY265
AGLU267
AGLU267
ATHR405
ATHR405
AGLY406
AGLY406
AHOH683
AHOH683

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 506
ChainResidue
AARG344
AASP355
AGLN377
AGLN377

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

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PDB entries from 2024-07-17

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