MolNFT v1 · #117276 · protein
Redox protein from chlamydomonas reinhardtii
5E37 · Ef-hand domain-containing thioredoxin: “Redox protein from chlamydomonas reinhardtii”. X-ray diffraction, 1 ligand (CA), 5 pockets (best druggability 0.63). MolNFT v1 #117276 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5E37
- Type
- protein
- Length
- 623 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ef-hand domain-containing thioredoxin
- Ligands
- CA
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ef-hand domain-containing thioredoxin | protein | 313 | 46% helix, 11% strand | — |
| C | Ef-hand domain-containing thioredoxin | protein | 310 | 46% helix, 12% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 532 | 0.63 | 0.75 | 51 | empty |
| 2 | 165 | 0.45 | 0.75 | 18 | empty |
| 3 | 112 | 0.43 | 0.77 | 18 | empty |
| 4 | 108 | 0.41 | 0.77 | 22 | empty |
| 5 | 75 | 0.37 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–C · 586 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5E37 · Redox protein from Chlamydomonas reinhardtii · 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
- Elsewhere: RCSB PDB 5E37 · PDBe 5E37
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