Research workbench
Crystal structure of VNG1086C from halobacterium salinarium (halobacterium halobium). northeast structural genomics target HSR14
Analyse Crystal structure of VNG1086C from halobacterium salinarium (halobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GF4
- Type
- protein
- Length
- 164 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein VNG1086C
- UniProt
- Q9HQM9
- Ligands
- CA
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein VNG1086C | protein | 89 | 71% helix, 0% strand | Q9HQM9 |
| B | Protein VNG1086C | protein | 75 | 68% helix, 0% strand | Q9HQM9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 372 | 0.62 | 0.77 | 36 | empty |
| 2 | 63 | 0.31 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 633 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 2GF4 · Crystal structure of Vng1086c from Halobacterium salinarium (Halobacterium halobium).… · 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 Q9HQM9
- Elsewhere: RCSB PDB 2GF4 · PDBe 2GF4 · UniProt Q9HQM9
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