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2HBU

Crystal structure of HIF prolyl hydroxylase EGLN-1 in complex with a biologically active inhibitor

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 FE2 A 900
ChainResidue
AUN91
AHIS313
AASP315
AHIS374
AHOH993

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UN9 A 1
ChainResidue
AHIS313
AASP315
ATYR329
ALEU343
AHIS374
AVAL376
AARG383
AARG398
AFE2900
AHOH921
AHOH993
AASP254
AMET299
ATYR303
ATYR310

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

222036

PDB entries from 2024-07-03

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