Research workbench
Transportin 3 in complex with RAN(Q69L)GTP
Analyse Transportin 3 in complex with RAN(Q69L)GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C0Q
- Type
- protein
- Length
- 1,964 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transportin-3; GTP-binding nuclear protein ran
- UniProt
- Q9Y5L0, P62826
- Ligands
- GTP, MG
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 68% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transportin-3 | protein | 871 | 76% helix, 0% strand | Q9Y5L0 |
| B | Transportin-3 | protein | 749 | 77% helix, 0% strand | Q9Y5L0 |
| C | GTP-binding nuclear protein ran | protein | 169 | 28% helix, 28% strand | P62826 |
| D | GTP-binding nuclear protein ran | protein | 175 | 27% helix, 27% strand | P62826 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, C, B, D
- MG · Magnesium ion · metal · 2 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1074 | 0.83 | 0.84 | 98 | MG, GTP |
| 2 | 972 | 0.82 | 0.84 | 119 | empty |
| 3 | 963 | 0.80 | 0.82 | 92 | MG, GTP |
| 4 | 1200 | 0.75 | 0.77 | 78 | empty |
| 5 | 349 | 0.62 | 0.78 | 39 | empty |
Interfaces
5 interfaces between chains.
- A–C · 2051 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 1980 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 521 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 486 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 58 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 42 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 Q9Y5L0
- Every structure of UniProt P62826
- Elsewhere: RCSB PDB 4C0Q · PDBe 4C0Q · UniProt Q9Y5L0 · UniProt P62826
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