Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2YC0

FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH R-2-HYDROXYGLUTARATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003714molecular_functiontranscription corepressor activity
A0005112molecular_functionNotch binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0019826molecular_functionoxygen sensor activity
A0031406molecular_functioncarboxylic acid binding
A0036139molecular_functionpeptidyl-histidine dioxygenase activity
A0036140molecular_function[protein]-asparagine 3-dioxygenase activity
A0042803molecular_functionprotein homodimerization activity
A0045663biological_processpositive regulation of myoblast differentiation
A0045746biological_processnegative regulation of Notch signaling pathway
A0045892biological_processnegative regulation of DNA-templated transcription
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0051059molecular_functionNF-kappaB binding
A0051213molecular_functiondioxygenase activity
A0062101molecular_functionpeptidyl-aspartic acid 3-dioxygenase activity
A0071532molecular_functionankyrin repeat binding
A2001214biological_processpositive regulation of vasculogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 501
ChainResidue
AHIS199
AASP201
AHIS279
A2HG601
AGOL604

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 2HG A 601
ChainResidue
AASN205
APHE207
ALYS214
AHIS279
AILE281
AASN294
ATRP296
AFE2501
AGOL604
ATYR145
ATHR196
AHIS199
AASP201

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
ALYS99
ALEU101
ATYR230
ASER240
AGLN241
AASP243
AHOH2091

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 603
ChainResidue
AASP222
ALYS315
AMET319

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 604
ChainResidue
ATYR102
AGLN147
ATHR196
AHIS199
AASP201
ATRP296
AFE2501
A2HG601

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AASP222
ALYS311
AALA312
AHOH2092
AHOH2093

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 902
ChainResidue
AARG138
AGLY140
AGLU141
AGLU142

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 904
ChainResidue
AARG120

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 905
ChainResidue
AARG143
AGLU192
AGLY193
ALEU285
AASN286

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:21251231
ChainResidueDetails
ATYR145
ATHR196
AASN205
ALYS214
AASN294

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:21177872
ChainResidueDetails
AASP152
AGLN181
AARG238
AALA300
AASN321

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:15913349, ECO:0000269|PubMed:17135241, ECO:0000269|PubMed:20396966, ECO:0000269|PubMed:20822901, ECO:0000269|PubMed:21251231, ECO:0000269|PubMed:21460794
ChainResidueDetails
AHIS199
AASP201
AHIS279

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for dimer formation
ChainResidueDetails
ALEU340

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2

225158

PDB entries from 2024-09-18

PDB statisticsPDBj update infoContact PDBjnumon