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1LQB

Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001222molecular_functiontranscription corepressor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006367biological_processtranscription initiation at RNA polymerase II promoter
A0006368biological_processtranscription elongation by RNA polymerase II
A0016567biological_processprotein ubiquitination
A0030891cellular_componentVCB complex
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0031466cellular_componentCul5-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0065003biological_processprotein-containing complex assembly
A0070449cellular_componentelongin complex
A0140958biological_processtarget-directed miRNA degradation
B0006511biological_processubiquitin-dependent protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
AALA73
ATHR74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine; by GSK3-beta => ECO:0000269|PubMed:20889502
ChainResidueDetails
DSER551

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by GSK3-beta => ECO:0000269|PubMed:20889502
ChainResidueDetails
DTHR555

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:25974097
ChainResidueDetails
DHYP564
ASER111

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PLK3 => ECO:0000269|PubMed:20889502
ChainResidueDetails
DSER576

218500

PDB entries from 2024-04-17

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