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The crystal structure of human rrad in complex with GDP
Analyse The crystal structure of human rrad in complex with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GJS
- Type
- protein
- Length
- 289 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-binding protein rad
- UniProt
- P55042
- Ligands
- GDP, MG
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP-binding protein rad | protein | 150 | 42% helix, 29% strand | P55042 |
| B | GTP-binding protein rad | protein | 139 | 40% helix, 29% strand | P55042 |
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
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.51 | 0.85 | 16 | empty |
| 2 | 102 | 0.43 | 0.78 | 23 | empty |
| 3 | 83 | 0.36 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 572 Ų buried · 1 hydrogen bond · 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 P55042
- Elsewhere: RCSB PDB 2GJS · PDBe 2GJS · UniProt P55042
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