Research workbench
Lysine 120-acetylated P53 DNA binding domain in a complex with the bax response element.
Analyse Lysine 120-acetylated P53 DNA binding domain in a complex with the bax response… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LGY
- Type
- protein + DNA
- Length
- 831 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular tumor antigen P53; DNA (5'- D(*TP*CP*AP*CP*AP*AP*GP*TP*TP*AP*GP*AP*GP*AP*CP*AP*AP…
- UniProt
- P04637
- Ligands
- ZN
- Pockets
- 17 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 9% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Cellular tumor antigen P53 | protein | 197 | 9% helix, 32% strand | P04637 |
| B | Cellular tumor antigen P53 | protein | 198 | 10% helix, 34% strand | P04637 |
| E | DNA (5'- D(*TP*CP*AP*CP*AP*AP*GP*TP*TP*AP*GP*AP*GP*AP*CP*AP*AP*GP*CP*CP*T)- 3') | dna | 21 | — | — |
| F | DNA (5'- D(*AP*GP*GP*CP*TP*TP*GP*TP*CP*TP*CP*TP*AP*AP*CP*TP*TP*GP*TP*GP*A)- 3') | dna | 21 | — | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 706 | 0.76 | 0.82 | 66 | empty |
| 2 | 407 | 0.75 | 0.85 | 33 | empty |
| 3 | 610 | 0.70 | 0.78 | 56 | empty |
| 4 | 276 | 0.56 | 0.77 | 28 | empty |
| 5 | 278 | 0.50 | 0.74 | 33 | empty |
Interfaces
13 interfaces between chains.
- E–F · 959 Ų buried · 99 hydrogen bonds · nucleic-nucleic
- A–C · 530 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 384 Ų buried · 0 hydrogen bonds · protein-protein
- C–E · 347 Ų buried · 7 hydrogen bonds · protein-nucleic
- A–B · 347 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (acetylation).
Compared structures
- 5LGY · Lysine 120-acetylated P53 DNA binding domain in a complex with the BAX response element. · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 5LGY · PDBe 5LGY · UniProt P04637
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