Research workbench
Canine GDP-ran
Analyse Canine GDP-ran in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BYU
- Type
- protein
- Length
- 417 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (GTP-binding protein ran)
- UniProt
- P62825
- Ligands
- GDP, MG
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (GTP-binding protein ran) | protein | 202 | 36% helix, 27% strand | P62825 |
| B | Protein (GTP-binding protein ran) | protein | 215 | 33% helix, 25% strand | P62825 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 848 | 0.69 | 0.75 | 59 | empty |
| 2 | 79 | 0.36 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 632 Ų buried · 5 hydrogen bonds · protein-protein
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 P62825
- Elsewhere: RCSB PDB 1BYU · PDBe 1BYU · UniProt P62825
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