Research workbench
Crystal structure of yeast GGA1_GAE domain-C2221
Analyse Crystal structure of yeast GGA1_GAE domain-C2221 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CN2
- Type
- protein
- Length
- 229 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor-binding protein GGA1
- UniProt
- Q06336
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor-binding protein GGA1 | protein | 115 | 3% helix, 62% strand | Q06336 |
| B | ADP-ribosylation factor-binding protein GGA1 | protein | 114 | 3% helix, 57% strand | Q06336 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 318 | 0.58 | 0.77 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 279 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 Q06336
- Elsewhere: RCSB PDB 5CN2 · PDBe 5CN2 · UniProt Q06336
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