6FJ5
New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-AGG-HG)
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 | 6 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
B | VAL97 |
A | THR231 |
A | HIS233 |
A | HOH403 |
A | HOH435 |
A | HOH522 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | LYS132 |
A | SER240 |
A | PRO250 |
A | VAL272 |
A | ARG273 |
A | HOH446 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | SER95 |
A | VAL97 |
A | HOH401 |
A | HOH404 |
B | THR231 |
B | HIS233 |
B | EDO304 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | CYS176 |
B | HIS179 |
B | CYS238 |
B | CYS242 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | LYS132 |
B | SER240 |
B | PRO250 |
B | VAL272 |
B | ARG273 |
B | HOH404 |
B | HOH455 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | LEU114 |
B | CYS124 |
B | PRO142 |
B | HOH506 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
A | SER95 |
A | VAL97 |
A | EDO304 |
B | VAL197 |
B | GLU198 |
B | GLY199 |
B | THR231 |
B | ILE232 |
B | HIS233 |
B | HOH431 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ZN C 301 |
Chain | Residue |
C | CYS176 |
C | HIS179 |
C | CYS238 |
C | CYS242 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
C | ARG110 |
C | LEU111 |
C | TRP146 |
C | HOH476 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
C | PHE113 |
C | LEU114 |
C | CYS124 |
C | THR125 |
C | TYR126 |
C | PRO142 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue EDO C 304 |
Chain | Residue |
C | LYS132 |
C | SER240 |
C | PRO250 |
C | VAL272 |
C | ARG273 |
C | GLU285 |
C | HOH492 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue EDO C 305 |
Chain | Residue |
C | PRO98 |
C | SER99 |
C | GLN100 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue ZN D 301 |
Chain | Residue |
D | CYS176 |
D | HIS179 |
D | CYS238 |
D | CYS242 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue EDO D 302 |
Chain | Residue |
D | ARG110 |
D | LEU111 |
D | TRP146 |
D | HOH496 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
D | PHE113 |
D | LEU114 |
D | CYS124 |
D | THR125 |
D | TYR126 |
D | PRO142 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue EDO D 304 |
Chain | Residue |
D | LYS132 |
D | SER240 |
D | PRO250 |
D | VAL272 |
D | ARG273 |
D | GLU285 |
D | HOH485 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue EDO D 305 |
Chain | Residue |
D | PRO98 |
D | SER99 |
D | GLN100 |
D | ILE162 |
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 binding: {"evidences":[{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18996393","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 492 |
Details | Region: {"description":"Required for interaction with FBXO42","evidences":[{"source":"PubMed","id":"19509332","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 704 |
Details | Region: {"description":"Interaction with AXIN1","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 28 |
Details | Region: {"description":"Interaction with the 53BP2 SH3 domain"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 28 |
Details | Region: {"description":"Interaction with DNA"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"14534297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17015838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18650397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19515728","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20142040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Site: {"description":"Interaction with DNA","evidences":[{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18996393","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | Modified residue: {"description":"N6-lactoyllysine","evidences":[{"source":"PubMed","id":"38653238","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | Modified residue: {"description":"Phosphoserine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphothreonine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 12 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"19536131","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |