6LHD
Crystal structure of p53/BCL-xL fusion complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000976 | molecular_function | transcription cis-regulatory region binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006915 | biological_process | apoptotic process |
| A | 0042981 | biological_process | regulation of apoptotic process |
| B | 0000976 | molecular_function | transcription cis-regulatory region binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006915 | biological_process | apoptotic process |
| B | 0042981 | biological_process | regulation of apoptotic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | CYS242 |
| A | HIS245 |
| A | CYS304 |
| A | CYS308 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | CYS242 |
| B | HIS245 |
| B | CYS304 |
| B | CYS308 |
Functional Information from PROSITE/UniProt
| site_id | PS00348 |
| Number of Residues | 13 |
| Details | P53 p53 family signature. MCNSSCMGGMNRR |
| Chain | Residue | Details |
| A | MET303-ARG315 |
| site_id | PS01080 |
| Number of Residues | 19 |
| Details | BH1 Apoptosis regulator, Bcl-2 family BH1 motif signature. LFrDGv.NWGRIVAFFsFGG |
| Chain | Residue | Details |
| A | LEU90-GLY108 |
| site_id | PS01258 |
| Number of Residues | 12 |
| Details | BH2 Apoptosis regulator, Bcl-2 family BH2 motif signature. WIqenGGWDtFV |
| Chain | Residue | Details |
| A | TRP141-VAL149 |
| site_id | PS01259 |
| Number of Residues | 15 |
| Details | BH3 Apoptosis regulator, Bcl-2 family BH3 motif signature. VkqaLReAGDEFELR |
| Chain | Residue | Details |
| A | VAL46-ARG60 |
| site_id | PS01260 |
| Number of Residues | 21 |
| Details | BH4_1 Apoptosis regulator, Bcl-2 family BH4 motif signature. SNRELVvDFLSYKLSQKGYsW |
| Chain | Residue | Details |
| A | SER4-TRP24 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by caspase-1 |
| Chain | Residue | Details |
| A | TYR61 | |
| B | TYR61 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PLK3 => ECO:0000269|PubMed:21840391 |
| Chain | Residue | Details |
| A | ALA49 | |
| B | ALA49 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:19917720 |
| Chain | Residue | Details |
| A | ARG62 | |
| B | ARG62 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130 |
| Chain | Residue | Details |
| A | SER281 | |
| A | VAL284 | |
| A | CYS343 | |
| A | ASP347 | |
| B | SER281 | |
| B | VAL284 | |
| B | CYS343 | |
| B | ASP347 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 |
| Chain | Residue | Details |
| A | ALA225 | |
| B | ALA225 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171 |
| Chain | Residue | Details |
| A | ALA225 | |
| B | ALA225 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 |
| Chain | Residue | Details |
| A | PRO288 | |
| B | PRO288 |
