7EEU
Human p53 core domain with hot spot mutation R282W in complex with the natural CDKN1A(p21) p53-response element and Arsenic
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 |
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 |
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 |
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 |
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 |
F | 0000976 | molecular_function | transcription cis-regulatory region binding |
F | 0003677 | molecular_function | DNA binding |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0005634 | cellular_component | nucleus |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0006915 | biological_process | apoptotic process |
G | 0000976 | molecular_function | transcription cis-regulatory region binding |
G | 0003677 | molecular_function | DNA binding |
G | 0003700 | molecular_function | DNA-binding transcription factor activity |
G | 0005634 | cellular_component | nucleus |
G | 0006355 | biological_process | regulation of DNA-templated transcription |
G | 0006915 | biological_process | apoptotic process |
H | 0000976 | molecular_function | transcription cis-regulatory region binding |
H | 0003677 | molecular_function | DNA binding |
H | 0003700 | molecular_function | DNA-binding transcription factor activity |
H | 0005634 | cellular_component | nucleus |
H | 0006355 | biological_process | regulation of DNA-templated transcription |
H | 0006915 | biological_process | apoptotic process |
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 | 1520 |
Details | DNA_BIND: DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 |
Chain | Residue | Details |
A | THR102-LYS292 | |
B | THR102-LYS292 | |
C | THR102-LYS292 | |
D | THR102-LYS292 | |
E | THR102-LYS292 | |
F | THR102-LYS292 | |
G | THR102-LYS292 | |
H | THR102-LYS292 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
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 | |
C | HIS179 | |
C | CYS238 | |
C | CYS242 | |
D | CYS176 | |
D | HIS179 | |
D | CYS238 | |
D | CYS242 | |
E | CYS176 | |
E | HIS179 | |
E | CYS238 | |
A | HIS179 | |
E | CYS242 | |
F | CYS176 | |
F | HIS179 | |
F | CYS238 | |
F | CYS242 | |
G | CYS176 | |
G | HIS179 | |
G | CYS238 | |
G | CYS242 | |
H | CYS176 | |
A | CYS238 | |
H | HIS179 | |
H | CYS238 | |
H | CYS242 | |
A | CYS242 | |
B | CYS176 | |
B | HIS179 | |
B | CYS238 | |
B | CYS242 | |
C | CYS176 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
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 | |
E | LYS120 | |
F | LYS120 | |
G | LYS120 | |
H | LYS120 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171 |
Chain | Residue | Details |
A | LYS120 | |
B | LYS120 | |
C | LYS120 | |
D | LYS120 | |
E | LYS120 | |
F | LYS120 | |
G | LYS120 | |
H | LYS120 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 |
Chain | Residue | Details |
A | SER183 | |
E | SER269 | |
F | SER183 | |
F | SER269 | |
G | SER183 | |
G | SER269 | |
H | SER183 | |
H | SER269 | |
A | SER269 | |
B | SER183 | |
B | SER269 | |
C | SER183 | |
C | SER269 | |
D | SER183 | |
D | SER269 | |
E | SER183 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 |
Chain | Residue | Details |
A | THR284 | |
B | THR284 | |
C | THR284 | |
D | THR284 | |
E | THR284 | |
F | THR284 | |
G | THR284 | |
H | THR284 |
site_id | SWS_FT_FI7 |
Number of Residues | 24 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131 |
Chain | Residue | Details |
A | LYS291 | |
D | LYS291 | |
D | LYS292 | |
E | LYS291 | |
E | LYS292 | |
F | LYS291 | |
F | LYS292 | |
G | LYS291 | |
G | LYS292 | |
H | LYS291 | |
H | LYS292 | |
A | LYS292 | |
B | LYS291 | |
B | LYS292 | |
C | LYS291 | |
C | LYS292 |