6GFY
pVHL:EloB:EloC in complex with modified VH032 containing (3R,4S)-3-fluoro-4-hydroxyproline (ligand 14a)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006368 | biological_process | transcription elongation by RNA polymerase II |
| A | 0030891 | cellular_component | VCB complex |
| A | 0070449 | cellular_component | elongin complex |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| D | 0006368 | biological_process | transcription elongation by RNA polymerase II |
| D | 0030891 | cellular_component | VCB complex |
| D | 0070449 | cellular_component | elongin complex |
| E | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| G | 0006368 | biological_process | transcription elongation by RNA polymerase II |
| G | 0030891 | cellular_component | VCB complex |
| G | 0070449 | cellular_component | elongin complex |
| H | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| J | 0006368 | biological_process | transcription elongation by RNA polymerase II |
| J | 0030891 | cellular_component | VCB complex |
| J | 0070449 | cellular_component | elongin complex |
| K | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue EXH C 301 |
| Chain | Residue |
| C | TRP88 |
| C | TRP117 |
| C | HOH406 |
| C | HOH408 |
| C | PHE91 |
| C | TYR98 |
| C | PRO99 |
| C | ILE109 |
| C | HIS110 |
| C | SER111 |
| C | TYR112 |
| C | HIS115 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue EXH F 301 |
| Chain | Residue |
| F | TRP88 |
| F | PHE91 |
| F | TYR98 |
| F | PRO99 |
| F | ILE109 |
| F | HIS110 |
| F | SER111 |
| F | TYR112 |
| F | HIS115 |
| F | TRP117 |
| F | HOH401 |
| F | HOH414 |
| I | ARG182 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue EXH I 301 |
| Chain | Residue |
| F | ARG182 |
| I | TRP88 |
| I | TYR98 |
| I | PRO99 |
| I | ARG107 |
| I | ILE109 |
| I | HIS110 |
| I | SER111 |
| I | TYR112 |
| I | HIS115 |
| I | TRP117 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue EXH L 301 |
| Chain | Residue |
| C | ARG182 |
| L | TRP88 |
| L | PHE91 |
| L | TYR98 |
| L | PRO99 |
| L | ARG107 |
| L | ILE109 |
| L | HIS110 |
| L | SER111 |
| L | TYR112 |
| L | HIS115 |
| L | TRP117 |
| L | HOH405 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | MET1 | |
| D | MET1 | |
| G | MET1 | |
| J | MET1 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62869 |
| Chain | Residue | Details |
| A | THR84 | |
| D | THR84 | |
| G | THR84 | |
| J | THR84 |
