Research workbench
The crystal structure of human rerg in the GDP bound state
Analyse The crystal structure of human rerg in the GDP bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ATV
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-like estrogen-regulated growth inhibitor
- UniProt
- Q96A58
- Ligands
- GDP, MG
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-like estrogen-regulated growth inhibitor | protein | 168 | 41% helix, 24% strand | Q96A58 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.43 | 0.78 | 25 | MG, GDP |
Compared structures
- 2ATV · The crystal structure of human RERG in the GDP bound state · the same entry in another collection · chain A against A, TM-score 1.00
- Q96A58 · AlphaFold monomer V2.0 prediction for RAS-related and estrogen- regulated growth… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q96A58
- Elsewhere: RCSB PDB 2ATV · PDBe 2ATV · UniProt Q96A58
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