Research workbench
AlphaFold monomer V2.0 prediction for DNA ligase (P26996)
Analyse AlphaFold monomer V2.0 prediction for DNA ligase (P26996) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P26996
- Type
- protein
- Length
- 676 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x52dd39a1F0b0b49aB790E19FD5d5b8d2eb36C77b
- UniProt
- P26996
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 676 | — | P26996 |
Compared structures
- 1L7B · Solution NMR Structure of BRCT Domain of T. Thermophilus: Northeast Structural Genomics… · an experimental structure of the same protein · chain A against A, TM-score 0.11
- 1L7B · Solution NMR structure of brct domain of T. thermophilus: northeast structural genomics… · an experimental structure of the same protein · chain A against A, TM-score 0.11
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 P26996
- Elsewhere: UniProt P26996 · AlphaFold DB P26996
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