MolNFT v1 · #46295 · protein
The structure of the C-terminal domain of VIK1 has a motor domain fold but lacks a nucleotide-binding site.
2O0A: “The structure of the C-terminal domain of VIK1 has a motor domain fold but lacks a nucleotide-binding site.”. X-ray diffraction. MolNFT v1 #46295 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2O0A
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q12045
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 269 | — | Q12045 |
Compared structures
- 2O0A · The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12045 · AlphaFold monomer V2.0 prediction for spindle pole body-associated protein VIK1 (Q12045) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q12045
- Elsewhere: RCSB PDB 2O0A · PDBe 2O0A · UniProt Q12045
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