6HR2
Crystal structure of PROTAC 2 in complex with the bromodomain of human SMARCA4 and pVHL:ElonginC:ElonginB
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0016586 | cellular_component | RSC-type complex |
| C | 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 | 0006338 | biological_process | chromatin remodeling |
| E | 0016586 | cellular_component | RSC-type complex |
| G | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| H | 0006368 | biological_process | transcription elongation by RNA polymerase II |
| H | 0030891 | cellular_component | VCB complex |
| H | 0070449 | cellular_component | elongin complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | binding site for residue FWZ B 301 |
| Chain | Residue |
| A | VAL1484 |
| A | ILE1546 |
| A | HOH1601 |
| B | ARG69 |
| B | TRP88 |
| B | PHE91 |
| B | TYR98 |
| B | PRO99 |
| B | ARG107 |
| B | ILE109 |
| B | HIS110 |
| A | PHE1485 |
| B | SER111 |
| B | TYR112 |
| B | HIS115 |
| B | TRP117 |
| B | DMS302 |
| B | HOH439 |
| B | HOH453 |
| A | LEU1488 |
| A | LEU1494 |
| A | TYR1497 |
| A | VAL1505 |
| A | ALA1536 |
| A | PHE1539 |
| A | ASN1540 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 302 |
| Chain | Residue |
| B | ILE109 |
| B | HIS110 |
| B | FWZ301 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue DMS E 1601 |
| Chain | Residue |
| E | ILE1546 |
| E | HOH1701 |
| E | HOH1703 |
| F | HIS110 |
| F | FWZ301 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | binding site for residue FWZ F 301 |
| Chain | Residue |
| E | VAL1484 |
| E | PHE1485 |
| E | LEU1488 |
| E | LEU1494 |
| E | TYR1497 |
| E | VAL1505 |
| E | ALA1536 |
| E | PHE1539 |
| E | ASN1540 |
| E | ILE1546 |
| E | DMS1601 |
| E | HOH1701 |
| F | ARG69 |
| F | TRP88 |
| F | PHE91 |
| F | TYR98 |
| F | PRO99 |
| F | ARG107 |
| F | ILE109 |
| F | HIS110 |
| F | SER111 |
| F | TYR112 |
| F | HIS115 |
| F | TRP117 |
| F | HOH439 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO F 302 |
| Chain | Residue |
| F | PRO154 |
| F | VAL155 |
| F | HOH429 |
| G | TYR83 |
| G | ASN85 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO H 201 |
| Chain | Residue |
| H | TYR45 |
| H | LEU88 |
Functional Information from PROSITE/UniProt
| site_id | PS00633 |
| Number of Residues | 58 |
| Details | BROMODOMAIN_1 Bromodomain signature. SevFiqlpSrkelp..EYYelIrkpVdfkkIkerirnhk..Yrslndlekdvml.LcqNAqtF |
| Chain | Residue | Details |
| A | SER1482-PHE1539 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 222 |
| Details | Domain: {"description":"Bromo","evidences":[{"source":"PROSITE-ProRule","id":"PRU00035","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Required for binding to 'Lys-15'-acetylated histone 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 110 |
| Details | Region: {"description":"Involved in binding to CCT complex"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | Region: {"description":"Interaction with Elongin BC complex"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 130 |
| Details | Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| 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_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
