6HAY
Crystal structure of PROTAC 1 in complex with the bromodomain of human SMARCA2 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 | 23 |
| Details | binding site for residue FX8 B 301 |
| Chain | Residue |
| A | VAL1408 |
| B | ARG69 |
| B | TRP88 |
| B | PHE91 |
| B | TYR98 |
| B | PRO99 |
| B | ARG107 |
| B | ILE109 |
| B | HIS110 |
| B | SER111 |
| B | TYR112 |
| A | PHE1409 |
| B | HIS115 |
| B | TRP117 |
| B | EDO304 |
| B | HOH429 |
| A | LEU1418 |
| A | TYR1421 |
| A | VAL1429 |
| A | ALA1460 |
| A | PHE1463 |
| A | ASN1464 |
| A | ILE1470 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | ARG161 |
| B | HOH404 |
| B | HOH421 |
| C | GLU92 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | GLY123 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| A | GLN1469 |
| B | ARG108 |
| B | ILE109 |
| B | HIS110 |
| B | FX8301 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue FMT B 305 |
| Chain | Residue |
| B | ARG210 |
| H | ASP48 |
| H | ILE90 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 201 |
| Chain | Residue |
| C | HIS68 |
| C | SER71 |
| C | MET75 |
| C | ILE99 |
| C | HOH320 |
| D | PHE93 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 202 |
| Chain | Residue |
| C | SER87 |
| F | ARG107 |
| F | ARG108 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 203 |
| Chain | Residue |
| C | ARG63 |
| C | GLU64 |
| C | ILE65 |
| C | PHE109 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 201 |
| Chain | Residue |
| D | ASP40 |
| D | GLU41 |
| D | ARG80 |
| D | ALA81 |
| D | ASP82 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 202 |
| Chain | Residue |
| D | ASP48 |
| D | LEU88 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 203 |
| Chain | Residue |
| D | LEU88 |
| D | CYS89 |
| D | ILE90 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 204 |
| Chain | Residue |
| D | ASP47 |
| D | THR74 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 205 |
| Chain | Residue |
| D | THR23 |
| D | PHE25 |
| D | GLU26 |
| D | ASP53 |
| D | GLY54 |
| D | HOH303 |
| F | ARG176 |
| F | TYR185 |
| site_id | AD5 |
| Number of Residues | 26 |
| Details | binding site for residue FX8 F 301 |
| Chain | Residue |
| E | VAL1408 |
| E | PHE1409 |
| E | LEU1412 |
| E | TYR1421 |
| E | VAL1429 |
| E | ALA1460 |
| E | PHE1463 |
| E | ASN1464 |
| E | ILE1470 |
| E | HOH1506 |
| 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 | EDO304 |
| F | EDO305 |
| F | HOH425 |
| F | HOH438 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO F 302 |
| Chain | Residue |
| G | GLU92 |
| F | PRO81 |
| F | HOH401 |
| F | HOH415 |
| F | HOH449 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO F 303 |
| Chain | Residue |
| F | THR124 |
| F | ASP126 |
| F | GLN164 |
| F | ARG167 |
| F | PRO192 |
| F | HOH410 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO F 304 |
| Chain | Residue |
| E | GLN1469 |
| F | ILE109 |
| F | HIS110 |
| F | FX8301 |
| F | EDO305 |
| site_id | AD9 |
| Number of Residues | 9 |
| Details | binding site for residue EDO F 305 |
| Chain | Residue |
| E | SER1468 |
| E | GLN1469 |
| E | ILE1470 |
| E | HOH1506 |
| F | HIS110 |
| F | TYR112 |
| F | FX8301 |
| F | EDO304 |
| F | HOH433 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue EPE F 306 |
| Chain | Residue |
| F | ASP179 |
| F | ILE180 |
| F | VAL181 |
| F | ARG182 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO G 201 |
| Chain | Residue |
| G | GLU64 |
| G | ILE65 |
| G | GLU102 |
| G | MET105 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO G 202 |
| Chain | Residue |
| F | SER80 |
| F | PRO81 |
| G | GLU89 |
| G | ILE90 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO G 203 |
| Chain | Residue |
| B | ARG108 |
| G | SER86 |
| G | SER87 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO H 201 |
| Chain | Residue |
| E | GLU1466 |
| F | PRO71 |
| H | ASP48 |
| H | GLN49 |
| H | LEU50 |
| H | EDO204 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO H 202 |
| Chain | Residue |
| H | LYS46 |
| H | ASP47 |
| H | ALA73 |
| H | THR74 |
| H | HOH309 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO H 203 |
| Chain | Residue |
| H | MET6 |
| H | PHE93 |
| H | HOH304 |
| H | HOH307 |
| H | HOH309 |
| site_id | AE8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO H 204 |
| Chain | Residue |
| H | EDO201 |
| H | HOH323 |
Functional Information from PROSITE/UniProt
| site_id | PS00633 |
| Number of Residues | 58 |
| Details | BROMODOMAIN_1 Bromodomain signature. SevFiqlpSrkelp..EYYelIrkpVdfkkIkerirnhk..Yrslgdlekdvml.LchNAqtF |
| Chain | Residue | Details |
| A | SER1406-PHE1463 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"39570797","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9E30","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"39570797","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9E31","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","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 |






