Research workbench
Structural insights into the catalysis mechanism of M. smegmatis antimutator protein MUTT2
Analyse Structural insights into the catalysis mechanism of M. smegmatis antimutator… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZRC
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative mutator protein MUTT2/NUDIX hydrolase
- UniProt
- I7FJF7
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative mutator protein MUTT2/NUDIX hydrolase | protein | 124 | 24% helix, 40% strand | I7FJF7 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 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 | 133 | 0.46 | 0.77 | 24 | empty |
Compared structures
- 5ZRC · Structural insights into the catalysis mechanism of M. smegmatis antimutator protein MutT2 · 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 I7FJF7
- Elsewhere: RCSB PDB 5ZRC · PDBe 5ZRC · UniProt I7FJF7
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