Research workbench
Crystal structure of alfalfa feruoyl coenzyme a 3-O-methyltransferase
Analyse Crystal structure of alfalfa feruoyl coenzyme a 3-O-methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SUS
- Type
- protein
- Length
- 908 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caffeoyl-CoA O-methyltransferase
- EC
- 2.1.1.104
- UniProt
- Q40313
- Ligands
- SAH, SPF, CA
- Pockets
- 10 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Caffeoyl-CoA O-methyltransferase (EC 2.1.1.104) | protein | 227 | 51% helix, 16% strand | Q40313 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 4 copies · chains A, B, C, D
- SPF · Sinapoyl coenzyme A · ligand · chains A
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 546 | 0.69 | 0.78 | 68 | CA, SAH |
| 2 | 418 | 0.65 | 0.79 | 48 | CA, SAH |
| 3 | 378 | 0.64 | 0.78 | 47 | CA, SAH |
| 4 | 394 | 0.62 | 0.77 | 57 | CA, SAH |
| 5 | 187 | 0.61 | 0.83 | 26 | empty |
Interfaces
2 interfaces between chains.
- A–C · 1889 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 61 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1SUS · Crystal structure of alfalfa feruoyl coenzyme A 3-O-methyltransferase · the same entry in another collection · chain D against D, TM-score 1.00
- Q40313 · AlphaFold monomer V2.0 prediction for caffeoyl-CoA O-methyltransferase (Q40313) · a predicted model of the same protein · chain A 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 Q40313
- Elsewhere: RCSB PDB 1SUS · PDBe 1SUS · UniProt Q40313
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