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6YVT

HIF prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with MD-253

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
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0031418molecular_functionL-ascorbic acid binding
C0005506molecular_functioniron ion binding
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0031418molecular_functionL-ascorbic acid binding
D0005506molecular_functioniron ion binding
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0031418molecular_functionL-ascorbic acid binding
E0005506molecular_functioniron ion binding
E0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E0031418molecular_functionL-ascorbic acid binding
F0005506molecular_functioniron ion binding
F0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
F0031418molecular_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
APW2502
AHOH605

site_idAC2
Number of Residues13
Detailsbinding site for residue PW2 A 502
ChainResidue
ATYR329
ALEU343
AHIS374
AVAL376
AARG383
AMN501
AHOH605
CLYS400
CVAL401
ATYR303
ATYR310
AHIS313
AASP315

site_idAC3
Number of Residues5
Detailsbinding site for residue MN B 501
ChainResidue
BHIS313
BASP315
BHIS374
BPW2502
BHOH607

site_idAC4
Number of Residues14
Detailsbinding site for residue PW2 B 502
ChainResidue
BILE251
BARG252
BMET299
BTYR303
BHIS313
BTYR329
BLEU343
BHIS374
BVAL376
BARG383
BMN501
BHOH601
BHOH607
FVAL401

site_idAC5
Number of Residues5
Detailsbinding site for residue MN C 501
ChainResidue
CHIS313
CASP315
CHIS374
CPW2502
CHOH607

site_idAC6
Number of Residues13
Detailsbinding site for residue PW2 C 502
ChainResidue
CMET299
CTYR303
CTYR310
CHIS313
CILE327
CTYR329
CHIS374
CVAL376
CARG383
CMN501
CHOH607
DVAL401
DLEU404

site_idAC7
Number of Residues5
Detailsbinding site for residue MN D 501
ChainResidue
DHIS313
DASP315
DHIS374
DPW2502
DHOH606

site_idAC8
Number of Residues16
Detailsbinding site for residue PW2 D 502
ChainResidue
ALYS400
AVAL401
DASP250
DARG252
DMET299
DTYR303
DTYR310
DHIS313
DTYR329
DLEU343
DHIS374
DVAL376
DARG383
DMN501
DHOH606
DHOH607

site_idAC9
Number of Residues5
Detailsbinding site for residue MN E 501
ChainResidue
EHIS313
EASP315
EHIS374
EPW2502
EHOH609

site_idAD1
Number of Residues12
Detailsbinding site for residue PW2 E 502
ChainResidue
BVAL401
EMET299
ETYR303
EHIS313
ETYR329
ELEU343
EHIS374
EVAL376
EARG383
EMN501
EHOH605
EHOH609

site_idAD2
Number of Residues2
Detailsbinding site for residue GOL E 503
ChainResidue
EVAL210
EASP211

site_idAD3
Number of Residues4
Detailsbinding site for residue SO4 E 504
ChainResidue
EASP355
EGLU357
ELYS359
EARG362

site_idAD4
Number of Residues5
Detailsbinding site for residue MN F 501
ChainResidue
FHIS313
FASP315
FHIS374
FPW2502
FHOH605

site_idAD5
Number of Residues10
Detailsbinding site for residue PW2 F 502
ChainResidue
ELYS400
FTYR303
FHIS313
FTYR329
FLEU343
FHIS374
FVAL376
FARG383
FMN501
FHOH605

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
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
BHIS313
BASP315
BHIS374
CHIS313
CASP315
CHIS374
DHIS313
DASP315
DHIS374
EHIS313
EASP315
EHIS374
FHIS313
FASP315
FHIS374
AHIS313
AASP315
AHIS374

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:19604478
ChainResidueDetails
BARG383
CARG383
DARG383
EARG383
FARG383
AARG383

site_idSWS_FT_FI3
Number of Residues30
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:21601578
ChainResidueDetails
BCYS201
BCYS208
BCYS302
BCYS323
BCYS326
CCYS201
CCYS208
CCYS302
CCYS323
CCYS326
DCYS201
DCYS208
DCYS302
DCYS323
DCYS326
ECYS201
ECYS208
ECYS302
ECYS323
ECYS326
FCYS201
FCYS208
FCYS302
FCYS323
FCYS326
ACYS201
ACYS208
ACYS302
ACYS323
ACYS326

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PDB entries from 2024-06-12

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