Research workbench
Thorarchaeota rab co-crystallized with GTP gamma-S
Analyse Thorarchaeota rab co-crystallized with GTP gamma-S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EZD
- Type
- protein
- Length
- 346 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chains: A,B
- UniProt
- A0A135VL07
- Ligands
- GDP, GSP
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chains: A,B | protein | 171 | 42% helix, 26% strand | A0A135VL07 |
| B | Chains: A,B | protein | 175 | 36% helix, 26% strand | A0A135VL07 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- GSP · 5'-guanosine-diphosphate-monothiophosphate · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.67 | 0.83 | 33 | empty |
| 2 | 240 | 0.50 | 0.74 | 28 | empty |
| 3 | 129 | 0.44 | 0.77 | 26 | GDP |
| 4 | 50 | 0.28 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1274 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 7EZD · Thorarchaeota Rab co-crystallized with GTP gamma-S · 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 A0A135VL07
- Elsewhere: RCSB PDB 7EZD · PDBe 7EZD · UniProt A0A135VL07
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