Research workbench
AlphaFold monomer V2.0 prediction for DNA repair protein complementing xp-G cells (P28715)
Analyse AlphaFold monomer V2.0 prediction for DNA repair protein complementing xp-G… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P28715
- Type
- protein
- Length
- 1,186 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1deF5d0757faedfe2A626225e579ACe5e2e425d2
- UniProt
- P28715
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1186 | — | P28715 |
Compared structures
- 6TUX · Human xpg-DNA, complex 2 · an experimental structure of the same protein · chain A against A, TM-score 0.26
- 6TUX · human XPG-DNA, Complex 2 · an experimental structure of the same protein · chain A against A, TM-score 0.26
- 6TUR · human XPG, Apo1 form · an experimental structure of the same protein · chain A against BBB, TM-score 0.26
- 6TUW · human XPG-DNA, Complex 1 · an experimental structure of the same protein · chain A against A, TM-score 0.25
- 6TUW · Human xpg-DNA, complex 1 · an experimental structure of the same protein · chain A against A, TM-score 0.25
- 6VBH · Human XPG endonuclease catalytic domain · an experimental structure of the same protein · chain A against A, TM-score 0.25
- 6VBH · Human xpg endonuclease catalytic domain · an experimental structure of the same protein · chain A against A, TM-score 0.25
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 P28715
- Elsewhere: UniProt P28715 · AlphaFold DB P28715
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