Research workbench
Redox protein from chlamydomonas reinhardtii
Analyse Redox protein from chlamydomonas reinhardtii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J13
- Type
- protein
- Length
- 1,631 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-cys peroxiredoxin
- EC
- 1.11.1.-
- UniProt
- Q9FE86
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F, G, I | 2-cys peroxiredoxin (EC 1.11.1.-) | protein | 163 | 29% helix, 28% strand | Q9FE86 |
| E | 2-cys peroxiredoxin (EC 1.11.1.-) | protein | 162 | 30% helix, 28% strand | Q9FE86 |
| H, J | 2-cys peroxiredoxin (EC 1.11.1.-) | protein | 164 | 30% helix, 27% strand | Q9FE86 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.77 | 0.98 | 25 | empty |
| 2 | 100 | 0.77 | 0.97 | 28 | empty |
| 3 | 116 | 0.76 | 0.96 | 30 | empty |
| 4 | 151 | 0.75 | 0.93 | 41 | empty |
| 5 | 653 | 0.69 | 0.78 | 59 | empty |
Interfaces
9 interfaces between chains.
- I–J · 1051 Ų buried · 15 hydrogen bonds · protein-protein
- G–H · 1043 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1042 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1036 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 748 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6J13 · 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
- Every structure of UniProt Q9FE86
- Elsewhere: RCSB PDB 6J13 · PDBe 6J13 · UniProt Q9FE86
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