Research workbench
AlphaFold monomer V2.0 prediction for DNA replication licensing factor mcm-4 (Q95XQ8)
Analyse AlphaFold monomer V2.0 prediction for DNA replication licensing factor mcm-4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q95XQ8
- Type
- protein
- Length
- 823 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- UniProt
- Q95XQ8
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 823 | — | Q95XQ8 |
Compared structures
- 8OUW · Cryo-EM structure of CMG helicase bound to TIM-1/TIPN-1 and homodimeric DNSN-1 on fork… · an experimental structure of the same protein · chain A against 4, TM-score 0.72
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 Q95XQ8
- Elsewhere: UniProt Q95XQ8 · AlphaFold DB Q95XQ8
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