5XZC
Cryo-EM structure of p300-p53 protein complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004402 | molecular_function | histone acetyltransferase activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| 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 | 0051262 | biological_process | protein tetramerization |
| C | 0000976 | molecular_function | transcription cis-regulatory region binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0006915 | biological_process | apoptotic process |
| C | 0051262 | biological_process | protein tetramerization |
| D | 0000976 | molecular_function | transcription cis-regulatory region binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0006915 | biological_process | apoptotic process |
| D | 0051262 | biological_process | protein tetramerization |
| E | 0000976 | molecular_function | transcription cis-regulatory region binding |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003700 | molecular_function | DNA-binding transcription factor activity |
| E | 0005634 | cellular_component | nucleus |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0006915 | biological_process | apoptotic process |
| E | 0051262 | biological_process | protein tetramerization |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 760 |
| Details | DNA_BIND: DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 |
| Chain | Residue | Details |
| B | THR102-LYS292 | |
| C | THR102-LYS292 | |
| D | THR102-LYS292 | |
| E | THR102-LYS292 | |
| A | TRP1466 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| 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 |
| B | CYS176 | |
| D | HIS179 | |
| D | CYS238 | |
| D | CYS242 | |
| E | CYS176 | |
| E | HIS179 | |
| E | CYS238 | |
| E | CYS242 | |
| B | HIS179 | |
| B | CYS238 | |
| B | CYS242 | |
| C | CYS176 | |
| C | HIS179 | |
| C | CYS238 | |
| C | CYS242 | |
| D | CYS176 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 |
| Chain | Residue | Details |
| B | LYS120 | |
| C | LYS120 | |
| D | LYS120 | |
| E | LYS120 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171 |
| Chain | Residue | Details |
| B | LYS120 | |
| C | LYS120 | |
| D | LYS120 | |
| E | LYS120 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 |
| Chain | Residue | Details |
| B | SER183 | |
| B | SER269 | |
| C | SER183 | |
| C | SER269 | |
| D | SER183 | |
| D | SER269 | |
| E | SER183 | |
| E | SER269 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 |
| Chain | Residue | Details |
| B | THR284 | |
| C | THR284 | |
| D | THR284 | |
| E | THR284 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:12724314 |
| Chain | Residue | Details |
| B | LYS305 | |
| C | LYS305 | |
| D | LYS305 | |
| E | LYS305 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by AURKA, CDK1 and CDK2 => ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:14702041 |
| Chain | Residue | Details |
| B | SER315 | |
| C | SER315 | |
| D | SER315 | |
| E | SER315 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P02340 |
| Chain | Residue | Details |
| B | LYS321 | |
| C | LYS321 | |
| D | LYS321 | |
| E | LYS321 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:19011621 |
| Chain | Residue | Details |
| B | ARG333 | |
| C | ARG333 | |
| D | ARG333 | |
| E | ARG333 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | MOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621 |
| Chain | Residue | Details |
| B | ARG335 | |
| B | ARG337 | |
| C | ARG335 | |
| C | ARG337 | |
| D | ARG335 | |
| D | ARG337 | |
| E | ARG335 | |
| E | ARG337 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131 |
| Chain | Residue | Details |
| B | LYS291 | |
| B | LYS292 | |
| C | LYS291 | |
| C | LYS292 | |
| D | LYS291 | |
| D | LYS292 | |
| E | LYS291 | |
| E | LYS292 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443 |
| Chain | Residue | Details |
| B | LYS351 | |
| C | LYS351 | |
| D | LYS351 | |
| E | LYS351 |
