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 |






