Research workbench
Plasmodium falciparum phosphoethanolamine methyltransferase D128A mutant in complex with S-adenosylhomocysteine and phosphoethanolamine
Analyse Plasmodium falciparum phosphoethanolamine methyltransferase D128A mutant in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R6X
- Type
- protein
- Length
- 516 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoethanolamine N-methyltransferase
- UniProt
- Q6T755
- Ligands
- OPE, SAH
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoethanolamine N-methyltransferase | protein | 258 | 49% helix, 21% strand | Q6T755 |
Ligands and binding sites
- OPE · Phosphoric acid mono-(2-amino-ethyl) ester · ligand · 2 copies · chains A, B
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.78 | 0.92 | 40 | SAH |
| 2 | 428 | 0.77 | 0.86 | 65 | OPE, SAH |
| 3 | 225 | 0.59 | 0.80 | 32 | OPE |
| 4 | 119 | 0.43 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 358 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4R6X · Plasmodium falciparum phosphoethanolamine methyltransferase D128A mutant in complex with… · the same entry in another collection · chain B against B, 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 Q6T755
- Elsewhere: RCSB PDB 4R6X · PDBe 4R6X · UniProt Q6T755
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