MolNFT v1 · #14690 · protein
Crystal structure of human GGA2 vhs domain
1MHQ · ADP-ribosylation factor binding protein GGA2: “Crystal structure of human GGA2 vhs domain”. X-ray diffraction, 3 pockets (best druggability 0.62). MolNFT v1 #14690 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MHQ
- Type
- protein
- Length
- 287 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor binding protein GGA2
- UniProt
- Q9UJY4
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor binding protein GGA2 | protein | 143 | 69% helix, 0% strand | Q9UJY4 |
| B | ADP-ribosylation factor binding protein GGA2 | protein | 144 | 68% helix, 0% strand | Q9UJY4 |
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 | 285 | 0.62 | 0.79 | 43 | empty |
| 2 | 123 | 0.49 | 0.80 | 23 | empty |
| 3 | 119 | 0.41 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 743 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q9UJY4
- Elsewhere: RCSB PDB 1MHQ · PDBe 1MHQ · UniProt Q9UJY4
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