Research workbench
N-myristoyl transferase from candida albicans at 2.45 a
Analyse N-myristoyl transferase from candida albicans at 2.45 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NMT
- Type
- protein
- Length
- 1,173 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-myristoyl transferase
- EC
- 2.3.1.97
- UniProt
- P30418
- Pockets
- 13 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N-myristoyl transferase (EC 2.3.1.97) | protein | 392 | 29% helix, 30% strand | P30418 |
| C | N-myristoyl transferase (EC 2.3.1.97) | protein | 389 | 30% helix, 29% strand | P30418 |
Ligands and binding sites
- GOL · Glycerol · additive · 18 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1134 | 0.85 | 0.86 | 111 | GOL |
| 2 | 915 | 0.83 | 0.85 | 80 | GOL |
| 3 | 358 | 0.79 | 0.88 | 44 | GOL |
| 4 | 220 | 0.76 | 0.90 | 25 | empty |
| 5 | 549 | 0.68 | 0.78 | 65 | GOL |
Interfaces
2 interfaces between chains.
- A–B · 959 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 951 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1NMT · N-myristoyl transferase from candida albicans at 2.45 a · the same entry in another collection · chain A against A, TM-score 1.00
- P30418 · AlphaFold monomer V2.0 prediction for glycylpeptide N-tetradecanoyltransferase (P30418) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P30418
- Elsewhere: RCSB PDB 1NMT · PDBe 1NMT · UniProt P30418
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