Research workbench
Crystal structure of unliganded CRM1-ran-RANBP1
Analyse Crystal structure of unliganded CRM1-ran-RANBP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X2M
- Type
- protein
- Length
- 1,342 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-binding nuclear protein ran; Ran-specific GTPase-activating protein 1; Exportin-1
- UniProt
- P62826, P41920, P30822
- Ligands
- GNP, MG
- Pockets
- 15 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 64% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP-binding nuclear protein ran | protein | 208 | 28% helix, 22% strand | P62826 |
| B | Ran-specific GTPase-activating protein 1 | protein | 123 | 15% helix, 50% strand | P41920 |
| C | Exportin-1 | protein | 1011 | 77% helix, 1% strand | P30822 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 810 | 0.85 | 0.87 | 96 | empty |
| 2 | 825 | 0.68 | 0.75 | 62 | empty |
| 3 | 432 | 0.68 | 0.80 | 60 | empty |
| 4 | 361 | 0.65 | 0.80 | 39 | empty |
| 5 | 98 | 0.64 | 0.89 | 28 | GNP, MG |
Interfaces
3 interfaces between chains.
- A–C · 2196 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 2112 Ų buried · 32 hydrogen bonds · protein-protein
- B–C · 185 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 covalent (additive adduct).
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 P62826
- Every structure of UniProt P41920
- Every structure of UniProt P30822
- Elsewhere: RCSB PDB 6X2M · PDBe 6X2M · UniProt P62826 · UniProt P41920 · UniProt P30822
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