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 v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q84Y95, Q9FIC3
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 107 | — | Q84Y95 |
| B | — | protein | 80 | — | Q9FIC3 |
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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