Research workbench
The crystal structure of G4, the poxviral disulfide oxidoreductase essential for cytoplasmic disulfide bond formation
Analyse The crystal structure of G4, the poxviral disulfide oxidoreductase essential… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G2Q
- Type
- protein
- Length
- 345 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaredoxin-2
- UniProt
- P68460
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 3 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaredoxin-2 | protein | 115 | 37% helix, 25% strand | P68460 |
| B | Glutaredoxin-2 | protein | 121 | 36% helix, 24% strand | P68460 |
| C | Glutaredoxin-2 | protein | 109 | 32% helix, 23% strand | P68460 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 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 | 75 | 0.33 | 0.75 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 157 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 119 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 99 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2G2Q · The crystal structure of G4, the poxviral disulfide oxidoreductase essential for… · 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 P68460
- Elsewhere: RCSB PDB 2G2Q · PDBe 2G2Q · UniProt P68460
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