MolNFT v1 · #12352 · protein
Structure of a thermostable thymine-DNA glycosylase
1KEA · Possible G-T mismatches repair enzyme: “Structure of a thermostable thymine-DNA glycosylase”. X-ray diffraction, 3 ligands (SF4, ZN, CL), 1 pocket (best druggability 0.47). MolNFT v1 #12352 on GenesisL1: 3D structure, binding sites…
- PDB
- 1KEA
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Possible G-T mismatches repair enzyme
- EC
- 3.2.2.-
- UniProt
- P29588
- Ligands
- SF4, ZN, CL
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Possible G-T mismatches repair enzyme (EC 3.2.2.-) | protein | 217 | 65% helix, 0% strand | P29588 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- ZN · Zinc ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- ACT · Acetate ion · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 194 | 0.47 | 0.75 | 25 | empty |
Compared structures
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 P29588
- Elsewhere: RCSB PDB 1KEA · PDBe 1KEA · UniProt P29588
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