Research workbench
Leishmania major N-myristoyltransferase in complex with cofactor
Analyse Leishmania major N-myristoyltransferase in complex with cofactor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CGP
- Type
- protein
- Length
- 411 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycylpeptide N-tetradecanoyltransferase
- EC
- 2.3.1.97
- UniProt
- Q4Q5S8
- Ligands
- MYA, MG
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) | protein | 411 | 32% helix, 28% strand | Q4Q5S8 |
Ligands and binding sites
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 | 1009 | 0.79 | 0.80 | 75 | MYA, MG |
| 2 | 133 | 0.43 | 0.76 | 21 | empty |
Compared structures
- 4CGP · Leishmania major N-myristoyltransferase in complex with cofactor · 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 Q4Q5S8
- Elsewhere: RCSB PDB 4CGP · PDBe 4CGP · UniProt Q4Q5S8
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