Research workbench
Solution structure and DNA-binding properties of the phosphoesterase domain of DNA ligase D
Analyse Solution structure and DNA-binding properties of the phosphoesterase domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LJ6
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable ATP-dependent DNA ligase
- UniProt
- Q9I1X7
Structure
solution nmr · 1 distinct chain · 8% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable ATP-dependent DNA ligase | protein | 131 | 8% helix, 52% strand | Q9I1X7 |
Compared structures
- 2LJ6 · Solution Structure and DNA-binding Properties of the Phosphoesterase Domain of DNA Ligase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9I1X7 · AlphaFold monomer V2.0 prediction for multifunctional non-homologous end joining protein… · a predicted model of the same protein · chain A against A, TM-score 0.76
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 Q9I1X7
- Elsewhere: RCSB PDB 2LJ6 · PDBe 2LJ6 · UniProt Q9I1X7
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