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5LAT

HIF prolyl hydroxylase 2 (PHD2/EGLN1) P317R variant in complex with Mn(II) and N-[(1-chloro-4-hydroxyisoquinolin-3-yl)carbonyl]glycine (IOX3/UN9)

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
AUN9502
AHOH623

site_idAC2
Number of Residues15
Detailsbinding site for residue UN9 A 502
ChainResidue
AHIS313
AASP315
ATYR329
ALEU343
AHIS374
AVAL376
AARG383
AARG398
AMN501
AHOH620
AHOH623
AASP254
AMET299
ATYR303
ATYR310

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 503
ChainResidue
AGLN243
AASP250
AGLY288
ASER289
ATYR290
ATRP367
AARG371

site_idAC4
Number of Residues5
Detailsbinding site for residue BCT A 504
ChainResidue
AARG312
APRO373
AHOH604
AHOH605
AHOH612

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

223166

PDB entries from 2024-07-31

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