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3KCY

Factor inhibiting HIF-1 alpha in complex with 8-hydroxyquinoline

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 Residues4
DetailsBINDING SITE FOR RESIDUE FE2 A 1350
ChainResidue
AHQY1
AHIS199
AASP201
AHIS279

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1352
ChainResidue
AARG138
AGLY140
AGLU141
AGLU142

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1353
ChainResidue
AASP237
AARG320
ALYS324
AHOH386
ALYS107

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HQY A 1
ChainResidue
ALEU188
AHIS199
AASP201
AHIS279
AILE281
ATRP296
AFE21350

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

219140

PDB entries from 2024-05-01

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