MolNFT v1 · #91941 · protein
The structure of an AS(III) S-adenosylmethionine methyltransferase: insights into the mechanism of arsenic biotransformation
4FS8 · Arsenic methyltransferase: “The structure of an AS(III) S-adenosylmethionine methyltransferase: insights into the mechanism of arsenic…”. X-ray diffraction, 1 ligand (CA), 3 pockets (best druggability 0.56). MolNFT v1 #91941 on…
- PDB
- 4FS8
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arsenic methyltransferase
- UniProt
- C0JV69
- Ligands
- CA
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arsenic methyltransferase | protein | 323 | 35% helix, 24% strand | C0JV69 |
Ligands and binding sites
- CA · Calcium ion · metal · 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 | 199 | 0.56 | 0.79 | 31 | CA |
| 2 | 109 | 0.49 | 0.81 | 18 | empty |
| 3 | 100 | 0.36 | 0.74 | 26 | empty |
Compared structures
- 4FS8 · The structure of an As(III) S-adenosylmethionine methyltransferase: insights into the… · 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 C0JV69
- Elsewhere: RCSB PDB 4FS8 · PDBe 4FS8 · UniProt C0JV69
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