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Crystal structure (trigonal form) of C36S mutant of thioredoxin H1 from chlamydomonas reinhardtii
Analyse Crystal structure (trigonal form) of C36S mutant of thioredoxin H1 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q6V
- Type
- protein
- Length
- 224 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin H-type
- UniProt
- P80028
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Thioredoxin H-type | protein | 112 | 44% helix, 25% strand | P80028 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 608 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6Q6V · Crystal structure (trigonal form) of C36S mutant of thioredoxin h1 from Chlamydomonas… · the same entry in another collection · chain A against A, TM-score 1.00
- P80028 · AlphaFold monomer V2.0 prediction for thioredoxin H-type (P80028) · a predicted model of the same protein · chain A 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 P80028
- Elsewhere: RCSB PDB 6Q6V · PDBe 6Q6V · UniProt P80028
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