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X-ray crystal structure of a hypothetical deoxyuridine 5-triphosphate nucleotidohydrolase from mycobacterium abscessus
Analyse X-ray crystal structure of a hypothetical deoxyuridine 5-triphosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GK6
- Type
- protein
- Length
- 136 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- EC
- 3.6.1.23
- UniProt
- B1MCW0
- Ligands
- CL
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC 3.6.1.23) | protein | 136 | 3% helix, 36% strand | B1MCW0 |
Ligands and binding sites
- CL · Chloride ion · ion · 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 | 59 | 0.37 | 0.79 | 14 | empty |
Compared structures
- 4GK6 · X-ray crystal structure of a hypothetical deoxyuridine 5-triphosphate nucleotidohydrolase… · 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 B1MCW0
- Elsewhere: RCSB PDB 4GK6 · PDBe 4GK6 · UniProt B1MCW0
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