Research workbench
Catalytic domain of muty from escherichia COLI K20A mutant complexed to adenine
Analyse Catalytic domain of muty from escherichia COLI K20A mutant complexed to adenine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WEI
- Type
- protein
- Length
- 220 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
- ADE, SF4
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | A/G-specific adenine glycosylase (EC 3.2.2.-) | protein | 220 | 59% helix, 0% strand | P17802 |
Ligands and binding sites
- ADE · Adenine · ligand · chains A
- SF4 · Iron/sulfur cluster · ligand · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.69 | 0.94 | 20 | SF4 |
| 2 | 192 | 0.51 | 0.77 | 24 | ADE, EDO |
| 3 | 50 | 0.33 | 0.78 | 10 | empty |
| 4 | 54 | 0.25 | 0.73 | 14 | empty |
Compared structures
- 1WEI · Catalytic Domain Of Muty From Escherichia Coli K20A Mutant Complexed To Adenine · the same entry in another collection · chain A against A, TM-score 1.00
- P17802 · AlphaFold monomer V2.0 prediction for adenine DNA glycosylase (P17802) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 1WEI · PDBe 1WEI · UniProt P17802
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