4IBU
Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R in sequence-specific complex with DNA
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | CYS176 |
A | HIS179 |
A | CYS238 |
A | CYS242 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | LYS120 |
A | ARG280 |
A | HOH434 |
A | HOH462 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | SER240 |
A | ARG248 |
A | ARG249 |
A | PRO250 |
A | ILE251 |
A | GLU271 |
A | VAL272 |
A | CYS273 |
A | HOH454 |
A | HOH543 |
A | LYS132 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 304 |
Chain | Residue |
A | LEU130 |
A | ASN131 |
A | GLU271 |
B | SER95 |
B | SER96 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 305 |
Chain | Residue |
A | ALA138 |
A | ASP184 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 306 |
Chain | Residue |
A | LEU206 |
A | ASP208 |
A | ARG209 |
A | HOH654 |
C | SER116 |
F | DG12 |
F | HOH113 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 301 |
Chain | Residue |
B | CYS176 |
B | HIS179 |
B | CYS238 |
B | CYS242 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | LEU114 |
B | PRO142 |
B | HIS233 |
B | HOH459 |
B | HOH543 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 303 |
Chain | Residue |
B | ALA138 |
B | HOH454 |
B | HOH497 |
B | HOH577 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
B | SER185 |
B | ACT305 |
B | HOH561 |
D | GLY199 |
D | ASN200 |
D | GLU221 |
D | HOH445 |
D | HOH519 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT B 305 |
Chain | Residue |
B | SER183 |
B | ASP184 |
B | SER185 |
B | EDO304 |
B | HOH547 |
B | HOH561 |
D | HOH507 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 301 |
Chain | Residue |
C | CYS176 |
C | HIS179 |
C | CYS238 |
C | CYS242 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 302 |
Chain | Residue |
C | LEU114 |
C | PRO142 |
C | HIS233 |
C | HOH424 |
C | HOH617 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 303 |
Chain | Residue |
C | LEU130 |
C | LYS132 |
C | LYS164 |
C | GLU271 |
C | GLU285 |
C | HOH528 |
C | HOH639 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 304 |
Chain | Residue |
C | LEU130 |
C | ASN131 |
C | GLU271 |
C | HOH528 |
C | HOH650 |
D | SER96 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 301 |
Chain | Residue |
D | CYS176 |
D | HIS179 |
D | CYS238 |
D | CYS242 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 302 |
Chain | Residue |
B | LYS139 |
B | HOH413 |
D | ALA138 |
D | LYS139 |
D | THR140 |
D | GLU198 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 303 |
Chain | Residue |
D | PRO219 |
D | HOH422 |
D | HOH451 |
D | HOH551 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 304 |
Chain | Residue |
D | ASP207 |
D | HOH411 |
D | PRO190 |
D | TYR205 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 305 |
Chain | Residue |
D | LEU114 |
D | PRO142 |
D | THR231 |
D | HIS233 |
D | HOH446 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 306 |
Chain | Residue |
B | GLY187 |
B | LEU188 |
B | HOH537 |
D | LEU201 |
D | ARG202 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT H 101 |
Chain | Residue |
A | SER260 |
A | SER261 |
A | HOH580 |
C | ALA119 |
C | LYS120 |
H | DG2 |
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-LYS292 | |
B | THR102-LYS292 | |
C | THR102-LYS292 | |
D | THR102-LYS292 |
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 | |
C | HIS179 | |
C | CYS238 | |
C | CYS242 | |
D | CYS176 | |
D | HIS179 | |
D | CYS238 | |
D | CYS242 | |
A | HIS179 | |
A | CYS238 | |
A | CYS242 | |
B | CYS176 | |
B | HIS179 | |
B | CYS238 | |
B | CYS242 | |
C | 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 |
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 | ARG284 | |
B | ARG284 | |
C | ARG284 | |
D | ARG284 |
site_id | SWS_FT_FI7 |
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 | |
D | LYS291 | |
D | LYS292 | |
A | LYS292 | |
B | LYS291 | |
B | LYS292 | |
C | LYS291 | |
C | LYS292 |