1LQB
Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000151 | cellular_component | ubiquitin ligase complex |
| A | 0001222 | molecular_function | transcription corepressor binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
| A | 0006368 | biological_process | transcription elongation by RNA polymerase II |
| A | 0016567 | biological_process | protein ubiquitination |
| A | 0030891 | cellular_component | VCB complex |
| A | 0031462 | cellular_component | Cul2-RING ubiquitin ligase complex |
| A | 0031466 | cellular_component | Cul5-RING ubiquitin ligase complex |
| A | 0031625 | molecular_function | ubiquitin protein ligase binding |
| A | 0032436 | biological_process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
| A | 0065003 | biological_process | protein-containing complex assembly |
| A | 0070449 | cellular_component | elongin complex |
| A | 0140958 | biological_process | target-directed miRNA degradation |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 801 |
| Chain | Residue |
| A | ALA73 |
| A | THR74 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 65 |
| Details | Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 55 |
| Details | Region: {"description":"Involved in binding to CCT complex"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| Details | Region: {"description":"Interaction with Elongin BC complex"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"4-hydroxyproline","evidences":[{"source":"PubMed","id":"11292861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11566883","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12351678","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25974097","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
