MolNFT v1 · #53442 · protein
Structure of N-myristoyltransferase from L. donovani
2WUU: “Structure of N-myristoyltransferase from L. donovani”. X-ray diffraction, 1 ligand (NHW), 2 pockets (best druggability 0.76). MolNFT v1 #53442 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2WUU
- Type
- protein
- Length
- 402 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-myristoyltransferase
- EC
- 2.3.1.97
- UniProt
- A4I7H1
- Ligands
- NHW
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-myristoyltransferase (EC 2.3.1.97) | protein | 402 | 32% helix, 28% strand | A4I7H1 |
Ligands and binding sites
- NHW · 2-oxopentadecyl-CoA · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 830 | 0.76 | 0.79 | 86 | NHW |
| 2 | 140 | 0.41 | 0.74 | 27 | empty |
Compared structures
- 2WUU · Structure of N-myristoyltransferase from L. donovani · 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 A4I7H1
- Elsewhere: RCSB PDB 2WUU · PDBe 2WUU · UniProt A4I7H1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.