Research workbench
Crystal structure of glutaredoxin-like protein from aquifex aeolicus
Analyse Crystal structure of glutaredoxin-like protein from aquifex aeolicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YWM
- Type
- protein
- Length
- 911 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaredoxin-like protein
- UniProt
- O66753
- Pockets
- 11 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glutaredoxin-like protein | protein | 228 | 47% helix, 19% strand | O66753 |
| D | Glutaredoxin-like protein | protein | 227 | 46% helix, 19% strand | O66753 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 962 | 0.84 | 0.85 | 120 | empty |
| 2 | 128 | 0.57 | 0.83 | 17 | empty |
| 3 | 256 | 0.54 | 0.76 | 31 | empty |
| 4 | 241 | 0.54 | 0.77 | 24 | empty |
| 5 | 134 | 0.53 | 0.80 | 19 | empty |
Interfaces
5 interfaces between chains.
- B–D · 938 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 926 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 804 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 765 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 129 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified, 4 disulfide (engineered, disulfide).
Compared structures
- 2YWM · Crystal structure of glutaredoxin-like protein from Aquifex aeolicus · 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 O66753
- Elsewhere: RCSB PDB 2YWM · PDBe 2YWM · UniProt O66753
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