Research workbench
Crystal structure of MXR1 from saccharomyces cerevisiae in complex with TRX2
Analyse Crystal structure of MXR1 from saccharomyces cerevisiae in complex with TRX2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PIN
- Type
- protein
- Length
- 243 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin-2; Peptide methionine sulfoxide reductase
- EC
- 1.8.4.11
- UniProt
- P22803, P40029
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin-2 | protein | 104 | 37% helix, 31% strand | P22803 |
| B | Peptide methionine sulfoxide reductase (EC 1.8.4.11) | protein | 139 | 28% helix, 27% strand | P40029 |
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 | 238 | 0.51 | 0.76 | 43 | empty |
Interfaces
1 interface between chains.
- A–B · 496 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3PIN · Crystal structure of Mxr1 from Saccharomyces cerevisiae in complex with Trx2 · the same entry in another collection · chain B against B, TM-score 1.00
- P22803 · AlphaFold monomer V2.0 prediction for thioredoxin-2 (P22803) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P40029 · AlphaFold monomer V2.0 prediction for peptide methionine sulfoxide reductase (P40029) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P22803
- Every structure of UniProt P40029
- Elsewhere: RCSB PDB 3PIN · PDBe 3PIN · UniProt P22803 · UniProt P40029
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