Research workbench
NMR-based docking model of GrxS14-BolA2 apo-heterodimer from Arabidopsis thaliana
Analyse NMR-based docking model of GrxS14-BolA2 apo-heterodimer from Arabidopsis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MMA
- Type
- protein
- Length
- 187 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Source
- Arabidopsis thaliana
- Molecule
- Monothiol glutaredoxin-S14, chloroplastic; BolA2
- UniProt
- Q84Y95, Q9FIC3
- Pockets
- 2 · best druggability 0.34
Structure
solution nmr · resolution NOT · 2 distinct chains · 49% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Monothiol glutaredoxin-S14, chloroplastic | protein | 107 | 54% helix, 19% strand | Q84Y95 |
| B | BolA2 | protein | 80 | 43% helix, 26% strand | Q9FIC3 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.34 | 0.75 | 14 | empty |
| 2 | 59 | 0.33 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 830 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2MMA · NMR-based docking model of GRXS14-BOLA2 apo-heterodimer from arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
- Q84Y95 · AlphaFold monomer V2.0 prediction for monothiol glutaredoxin-S14, chloroplastic (Q84Y95) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9FIC3 · AlphaFold monomer V2.0 prediction for protein BOLA2 (Q9FIC3) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 Q84Y95
- Every structure of UniProt Q9FIC3
- Elsewhere: RCSB PDB 2MMA · PDBe 2MMA · UniProt Q84Y95 · UniProt Q9FIC3
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