Research workbench
NMR study of mutt enzyme, a nucleoside triphosphate pyrophosphohydrolase
Analyse NMR study of mutt enzyme, a nucleoside triphosphate pyrophosphohydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MUT
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoside triphosphate pyrophosphohydrolase
- EC
- 3.6.1.-
- UniProt
- P08337
- Pockets
- 1 · best druggability 0.37
Structure
solution nmr · 1 distinct chain · 12% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoside triphosphate pyrophosphohydrolase (EC 3.6.1.-) | protein | 129 | 12% helix, 23% strand | P08337 |
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 | 96 | 0.37 | 0.75 | 21 | empty |
Compared structures
- 1MUT · NMR study of mutt enzyme, a nucleoside triphosphate pyrophosphohydrolase · the same entry in another collection · chain A against A, TM-score 1.00
- P08337 · AlphaFold monomer V2.0 prediction for 8-oxo-dgtp diphosphatase (P08337) · a predicted model of the same protein · chain A against A, TM-score 0.68
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 P08337
- Elsewhere: RCSB PDB 1MUT · PDBe 1MUT · UniProt P08337
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