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Crystal structure of human GADD45GAMMA
Analyse Crystal structure of human GADD45GAMMA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WAL
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Growth arrest and DNA-damage-inducible protein GADD45 gamma
- UniProt
- O95257
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Growth arrest and DNA-damage-inducible protein GADD45 gamma | protein | 149 | 49% helix, 14% strand | O95257 |
| B | Growth arrest and DNA-damage-inducible protein GADD45 gamma | protein | 136 | 51% helix, 13% strand | O95257 |
Ligands and binding sites
- MLA · Malonic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.81 | 0.96 | 37 | empty |
| 2 | 63 | 0.69 | 0.96 | 16 | MLA |
| 3 | 76 | 0.64 | 0.92 | 23 | empty |
| 4 | 57 | 0.34 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1397 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
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 O95257
- Elsewhere: RCSB PDB 2WAL · PDBe 2WAL · UniProt O95257
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