MolNFT v1 · #37477 · protein
The crystal structure of G4, the poxviral disulfide oxidoreductase essential for cytoplasmic disulfide bond formation
2G2Q · Glutaredoxin-2: “The crystal structure of G4, the poxviral disulfide oxidoreductase essential for cytoplasmic disulfide bond…”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.33). MolNFT v1 #37477 on GenesisL1: 3D…
- 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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