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Crystal structure of autoinhibited form of GRP1 arf GTPase exchange factor
Analyse Crystal structure of autoinhibited form of GRP1 arf GTPase exchange factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R09
- Type
- protein
- Length
- 684 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytohesin-3
- UniProt
- O08967
- Ligands
- 4IP, SO4
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytohesin-3 | protein | 343 | 45% helix, 14% strand | O08967 |
| B | Cytohesin-3 | protein | 341 | 45% helix, 14% strand | O08967 |
Ligands and binding sites
- 4IP · Inositol-(1,3,4,5)-tetrakisphosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 7 copies · chains A, B
- PGE · Triethylene glycol · additive · chains A
- PE5 · 3,6,9,12,15,18,21,24-octaoxahexacosan-1-ol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 600 | 0.68 | 0.77 | 52 | PE5 |
| 2 | 344 | 0.64 | 0.80 | 42 | empty |
| 3 | 99 | 0.43 | 0.78 | 20 | 4IP |
| 4 | 96 | 0.39 | 0.76 | 17 | 4IP |
| 5 | 69 | 0.35 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 16 modified (engineered).
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 O08967
- Elsewhere: RCSB PDB 2R09 · PDBe 2R09 · UniProt O08967
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