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Solution structure of the AHA1 dimer from colwellia psychrerythraea
Analyse Solution structure of the AHA1 dimer from colwellia psychrerythraea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M89
- Type
- protein
- Length
- 268 residues
- Chains
- 2
- Method
- solution nmr; solution scattering
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AHA1 domain protein
- UniProt
- Q484T9
- Pockets
- 8 · best druggability 0.75
Structure
solution nmr; solution scattering · 1 distinct chain · 30% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | AHA1 domain protein | protein | 134 | 30% helix, 37% strand | Q484T9 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.75 | 0.96 | 24 | empty |
| 2 | 86 | 0.75 | 0.96 | 25 | empty |
| 3 | 203 | 0.57 | 0.79 | 19 | empty |
| 4 | 208 | 0.57 | 0.79 | 18 | empty |
| 5 | 86 | 0.54 | 0.85 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 685 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2M89 · Solution structure of the Aha1 dimer from Colwellia psychrerythraea · the same entry in another collection · chain A against A, TM-score 1.00
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 Q484T9
- Elsewhere: RCSB PDB 2M89 · PDBe 2M89 · UniProt Q484T9
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