1HU8
CRYSTAL STRUCTURE OF THE MOUSE P53 CORE DNA-BINDING DOMAIN AT 2.7A RESOLUTION
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | CYS173 |
A | HIS176 |
A | CYS235 |
A | CYS239 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 502 |
Chain | Residue |
B | CYS173 |
B | HIS176 |
B | CYS235 |
B | CYS239 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 503 |
Chain | Residue |
C | HIS176 |
C | CYS235 |
C | CYS239 |
C | CYS173 |
Functional Information from PROSITE/UniProt
site_id | PS00348 |
Number of Residues | 13 |
Details | P53 p53 family signature. MCNSSCMGGMNRR |
Chain | Residue | Details |
A | MET234-ARG246 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16717092 |
Chain | Residue | Details |
A | CYS173 | |
C | HIS176 | |
C | CYS235 | |
C | CYS239 | |
A | HIS176 | |
A | CYS235 | |
A | CYS239 | |
B | CYS173 | |
B | HIS176 | |
B | CYS235 | |
B | CYS239 | |
C | CYS173 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | SITE: Interaction with DNA => ECO:0000269|PubMed:16717092 |
Chain | Residue | Details |
A | LYS117 | |
B | LYS117 | |
C | LYS117 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine; by KAT6A => ECO:0000250|UniProtKB:P04637 |
Chain | Residue | Details |
A | LYS117 | |
B | LYS117 | |
C | LYS117 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine; by AURKB => ECO:0000250|UniProtKB:P04637 |
Chain | Residue | Details |
A | SER180 | |
A | SER266 | |
B | SER180 | |
B | SER266 | |
C | SER180 | |
C | SER266 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | MOD_RES: Phosphothreonine; by AURKB => ECO:0000250|UniProtKB:P04637 |
Chain | Residue | Details |
A | THR281 | |
B | THR281 | |
C | THR281 |