6GMR
pVHL:EloB:EloC in complex with (4-(1H-pyrrol-1-yl)phenyl)methanol
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0001222 | molecular_function | transcription corepressor binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
B | 0006368 | biological_process | transcription elongation by RNA polymerase II |
B | 0016567 | biological_process | protein ubiquitination |
B | 0030891 | cellular_component | VCB complex |
B | 0031462 | cellular_component | Cul2-RING ubiquitin ligase complex |
B | 0031466 | cellular_component | Cul5-RING ubiquitin ligase complex |
B | 0031625 | molecular_function | ubiquitin protein ligase binding |
B | 0032436 | biological_process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
B | 0065003 | biological_process | protein-containing complex assembly |
B | 0070449 | cellular_component | elongin complex |
B | 0140958 | biological_process | target-directed miRNA degradation |
C | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 201 |
Chain | Residue |
B | MET1 |
B | ASP2 |
B | PHE4 |
B | ARG68 |
C | ARG82 |
V | GLN132 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue F4K V 301 |
Chain | Residue |
V | GLU134 |
V | TYR156 |
V | GLU160 |
V | ASP197 |
V | HOH442 |
V | ARG120 |
V | GLY127 |
V | LEU128 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue GOL V 302 |
Chain | Residue |
V | ARG161 |
V | GLN164 |
V | HOH419 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:11292861, ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:25974097 |
Chain | Residue | Details |
H | HYP564 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PLK3 => ECO:0000269|PubMed:20889502 |
Chain | Residue | Details |
H | SER576 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62869 |
Chain | Residue | Details |
B | SER108 | |
B | SER111 |