MolNFT v1 · #128436 · protein
Mtb tmk crystal structure in complex with compound 1
5NQ5 · Thymidylate kinase: “Mtb tmk crystal structure in complex with compound 1”. X-ray diffraction, 1 ligand (952), 1 pocket (best druggability 0.55). MolNFT v1 #128436 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5NQ5
- Type
- protein
- Length
- 191 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate kinase
- EC
- 2.7.4.9
- UniProt
- P9WKE1
- Ligands
- 952
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidylate kinase (EC 2.7.4.9) | protein | 191 | 56% helix, 13% strand | P9WKE1 |
Ligands and binding sites
- 952 · 5-methyl-1-[(3~{S})-1-[(3-phenoxyphenyl) methyl]piperidin-3-yl]pyrimidine-2,4-dione · ligand · 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 | 200 | 0.55 | 0.79 | 26 | 952 |
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 P9WKE1
- Elsewhere: RCSB PDB 5NQ5 · PDBe 5NQ5 · UniProt P9WKE1
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