Research workbench
Crystal structure of glutamate O-methyltransferase in complex with S- adenosyl-L-homocysteine (sah) from bacillus subtilis
Analyse Crystal structure of glutamate O-methyltransferase in complex with S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FTW
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein methyltransferase
- EC
- 2.1.1.80
- UniProt
- P31105
- Ligands
- SAH, SO4
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis protein methyltransferase (EC 2.1.1.80) | protein | 255 | 47% helix, 22% strand | P31105 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- SO4 · Sulfate ion · ion · 6 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.77 | 0.95 | 29 | SAH |
| 2 | 55 | 0.32 | 0.77 | 16 | empty |
| 3 | 56 | 0.25 | 0.73 | 16 | empty |
Compared structures
- 5FTW · Crystal structure of glutamate O-methyltransferase in complex with S… · the same entry in another collection · chain A against A, TM-score 1.00
- P31105 · AlphaFold monomer V2.0 prediction for chemotaxis protein methyltransferase (P31105) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P31105
- Elsewhere: RCSB PDB 5FTW · PDBe 5FTW · UniProt P31105
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