3TS8
Crystal structure of a multidomain human p53 tetramer bound to the natural CDKN1A(p21) p53-response element
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 | 0051262 | biological_process | protein tetramerization |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1 |
Chain | Residue |
A | CYS176 |
A | HIS179 |
A | CYS238 |
A | CYS242 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1 |
Chain | Residue |
B | CYS176 |
B | HIS179 |
B | CYS238 |
B | CYS242 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 1 |
Chain | Residue |
C | HIS179 |
C | CYS238 |
C | CYS242 |
C | CYS176 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 1 |
Chain | Residue |
D | CYS176 |
D | HIS179 |
D | CYS238 |
D | CYS242 |
Functional Information from PROSITE/UniProt
site_id | PS00348 |
Number of Residues | 13 |
Details | P53 p53 family signature. MCNSSCMGGMNRR |
Chain | Residue | Details |
A | MET237-ARG249 |
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 |
A | THR102-LYS321 | |
B | THR102-LYS321 | |
C | THR102-LYS321 | |
D | THR102-LYS321 |
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 |
A | CYS176 | |
A | HIS179 | |
A | CYS238 | |
A | CYS242 | |
B | CYS176 | |
B | HIS179 | |
B | CYS238 | |
B | CYS242 | |
C | CYS176 | |
C | HIS179 | |
C | CYS238 | |
C | CYS242 | |
D | CYS176 | |
D | HIS179 | |
D | CYS238 | |
D | CYS242 |
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 |
A | LYS120 | |
B | LYS120 | |
C | LYS120 | |
D | LYS120 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171 |
Chain | Residue | Details |
A | LYS120 | |
B | LYS120 | |
C | LYS120 | |
D | LYS120 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 |
Chain | Residue | Details |
A | SER183 | |
A | SER269 | |
B | SER183 | |
B | SER269 | |
C | SER183 | |
C | SER269 | |
D | SER183 | |
D | SER269 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 |
Chain | Residue | Details |
A | THR284 | |
B | THR284 | |
C | THR284 | |
D | THR284 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:12724314 |
Chain | Residue | Details |
A | GLY334 | |
B | GLY334 | |
C | GLY334 | |
D | GLY334 |
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 |
A | ARG344 | |
B | ARG344 | |
C | ARG344 | |
D | ARG344 |
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 | |
A | 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 |
C | ARG333 | |
D | ARG333 | |
A | ARG333 | |
B | ARG333 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621 |
Chain | Residue | Details |
A | ARG337 | |
C | ARG335 | |
D | ARG337 | |
A | ARG335 | |
B | ARG335 | |
B | ARG337 | |
C | ARG337 | |
D | ARG335 |
site_id | SWS_FT_FI12 |
Number of Residues | 12 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131 |
Chain | Residue | Details |
A | LYS291 | |
A | LYS321 | |
B | LYS291 | |
B | LYS321 | |
C | LYS291 | |
C | LYS321 | |
D | LYS291 | |
D | LYS321 |