MolNFT v1 · #80428 · protein
Crystal structure of arabidopsis thaliana fpg
3TWK · Formamidopyrimidine-DNA glycosylase 1: “Crystal structure of arabidopsis thaliana fpg”. X-ray diffraction, 8 pockets (best druggability 0.54). MolNFT v1 #80428 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3TWK
- Type
- protein
- Length
- 579 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Formamidopyrimidine-DNA glycosylase 1
- EC
- 3.2.2.23
- UniProt
- Q9SBB4
- Pockets
- 8 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formamidopyrimidine-DNA glycosylase 1 (EC 3.2.2.23) | protein | 293 | 33% helix, 24% strand | Q9SBB4 |
| B | Formamidopyrimidine-DNA glycosylase 1 (EC 3.2.2.23) | protein | 286 | 31% helix, 22% strand | Q9SBB4 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.54 | 0.89 | 15 | empty |
| 2 | 55 | 0.53 | 0.87 | 14 | empty |
| 3 | 113 | 0.51 | 0.81 | 21 | empty |
| 4 | 57 | 0.47 | 0.85 | 19 | empty |
| 5 | 214 | 0.45 | 0.73 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 1294 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 3TWK · Crystal structure of arabidopsis thaliana FPG · 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 Q9SBB4
- Elsewhere: RCSB PDB 3TWK · PDBe 3TWK · UniProt Q9SBB4
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