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The crystal structure of a complex between the llfpg protein, a thf- DNA and an inhibitor
Analyse The crystal structure of a complex between the llfpg protein, a thf- DNA and an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ROK
- Type
- protein + DNA
- Length
- 299 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A165FVI1
- Ligands
- 5JL, ZN
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 271 | — | A0A165FVI1 |
| D | — | dna | 14 | — | — |
| E | — | dna | 14 | — | — |
Ligands and binding sites
- 5JL · 2,8-dithioxo-1,2,3,7,8,9-hexahydro-6H-purin-6-one · ligand · chains A, D
- ZN · Zinc ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ROK · The crystal structure of a complex between the LlFpg protein, a THF-DNA and an inhibitor · 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 A0A165FVI1
- Elsewhere: RCSB PDB 6ROK · PDBe 6ROK · UniProt A0A165FVI1
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