Research workbench
Crystal structure of DNA-binding domain of the bacteriophage T4 ligase
Analyse Crystal structure of DNA-binding domain of the bacteriophage T4 ligase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WFY
- Type
- protein
- Length
- 132 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA ligase
- EC
- 6.5.1.1
- UniProt
- P00970
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA ligase (EC 6.5.1.1) | protein | 132 | 57% helix, 2% strand | P00970 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 5WFY · Crystal structure of DNA-binding domain of the bacteriophage T4 ligase · the same entry in another collection · chain A against A, TM-score 1.00
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 P00970
- Elsewhere: RCSB PDB 5WFY · PDBe 5WFY · UniProt P00970
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