MolNFT v1 · #12750 · protein
Crystal structure of a mutant of muty catalytic domain
1KQJ · A/G-specific adenine glycosylase: “Crystal structure of a mutant of muty catalytic domain”. X-ray diffraction, 2 ligands (SF4, SO4), 1 pocket (best druggability 0.56). MolNFT v1 #12750 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1KQJ
- Type
- protein
- Length
- 225 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- A/G-specific adenine glycosylase
- EC
- 3.2.2.-
- UniProt
- P17802
- Ligands
- SF4, SO4
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | A/G-specific adenine glycosylase (EC 3.2.2.-) | protein | 225 | 62% helix, 0% strand | P17802 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 3 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.56 | 0.79 | 34 | 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 P17802
- Elsewhere: RCSB PDB 1KQJ · PDBe 1KQJ · UniProt P17802
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