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Crystal structure of human SAR1A in complex with GDP
Analyse Crystal structure of human SAR1A 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
- 2GAO
- Type
- protein
- Length
- 336 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-binding protein SAR1A
- UniProt
- Q9NR31
- Ligands
- GDP, UNX
- Pockets
- 3 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP-binding protein SAR1A | protein | 165 | 34% helix, 22% strand | Q9NR31 |
| B | GTP-binding protein SAR1A | protein | 171 | 31% helix, 21% strand | Q9NR31 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- UNX · Unknown atom or ion · ion · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.42 | 0.78 | 18 | empty |
| 2 | 99 | 0.39 | 0.76 | 21 | GDP |
| 3 | 57 | 0.33 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 423 Ų buried · 7 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 Q9NR31
- Elsewhere: RCSB PDB 2GAO · PDBe 2GAO · UniProt Q9NR31
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