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Crystal structure of thioredoxin E101G mutant
Analyse Crystal structure of thioredoxin E101G mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HR0
- Type
- protein
- Length
- 215 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin
- UniProt
- C3SKR2
- Ligands
- CU
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin | protein | 108 | 34% helix, 27% strand | C3SKR2 |
| B | Thioredoxin | protein | 107 | 33% helix, 26% strand | C3SKR2 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.49 | 0.80 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 423 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5HR0 · Crystal structure of thioredoxin E101G mutant · 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 C3SKR2
- Elsewhere: RCSB PDB 5HR0 · PDBe 5HR0 · UniProt C3SKR2
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