Research workbench
2ND crystal structure of a soluble domain of resa in the oxidised form
Analyse 2ND crystal structure of a soluble domain of resa in the oxidised form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F9S
- Type
- protein
- Length
- 274 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thiol-disulfide oxidoreductase resa
- UniProt
- P35160
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiol-disulfide oxidoreductase resa | protein | 138 | 37% helix, 28% strand | P35160 |
| B | Thiol-disulfide oxidoreductase resa | protein | 136 | 38% helix, 29% strand | P35160 |
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 | 282 | 0.54 | 0.76 | 47 | empty |
Interfaces
1 interface between chains.
- A–B · 287 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2F9S · 2nd Crystal Structure Of A Soluble Domain Of ResA In The Oxidised Form · the same entry in another collection · chain A against A, TM-score 1.00
- P35160 · AlphaFold monomer V2.0 prediction for thiol-disulfide oxidoreductase resa (P35160) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P35160
- Elsewhere: RCSB PDB 2F9S · PDBe 2F9S · UniProt P35160
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