Research workbench
Structure of the neck and C-terminal motor homology domain of VIK1 from candida glabrata
Analyse Structure of the neck and C-terminal motor homology domain of VIK1 from candida… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GKQ
- Type
- protein
- Length
- 456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spindle pole body-associated protein VIK1
- UniProt
- Q6FSG8
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spindle pole body-associated protein VIK1 | protein | 242 | 31% helix, 31% strand | Q6FSG8 |
| B | Spindle pole body-associated protein VIK1 | protein | 214 | 28% helix, 32% strand | Q6FSG8 |
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 | 197 | 0.50 | 0.76 | 21 | empty |
| 2 | 60 | 0.30 | 0.75 | 19 | empty |
Compared structures
- 4GKQ · Structure of the neck and C-terminal motor homology domain of ViK1 from Candida glabrata · 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 Q6FSG8
- Elsewhere: RCSB PDB 4GKQ · PDBe 4GKQ · UniProt Q6FSG8
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