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Crystal structure of selenoprotein W-related protein from vibrio cholerae. northeast structural genomics target VCR75
Analyse Crystal structure of selenoprotein W-related protein from vibrio cholerae.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P0G
- Type
- protein
- Length
- 318 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Selenoprotein W-related protein
- UniProt
- Q9KTC1
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 3 distinct chains · 34% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Selenoprotein W-related protein | protein | 78 | 35% helix, 35% strand | Q9KTC1 |
| B, C | Selenoprotein W-related protein | protein | 80 | 34% helix, 34% strand | Q9KTC1 |
| D | Selenoprotein W-related protein | protein | 80 | 34% helix, 34% strand | Q9KTC1 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.54 | 0.82 | 21 | empty |
| 2 | 99 | 0.53 | 0.83 | 19 | empty |
| 3 | 91 | 0.48 | 0.82 | 23 | empty |
| 4 | 100 | 0.48 | 0.81 | 22 | empty |
Interfaces
6 interfaces between chains.
- A–B · 806 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 799 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 538 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 514 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 92 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 4 modified (disulfide, engineered).
Compared structures
- 2P0G · Crystal structure of Selenoprotein W-related protein from Vibrio cholerae. Northeast… · 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 Q9KTC1
- Elsewhere: RCSB PDB 2P0G · PDBe 2P0G · UniProt Q9KTC1
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