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X-ray crystal structure of crarsm, an arsenic (III) S- adenosylmethionine methyltransferase from chlamydomonas reinhardtii
Analyse X-ray crystal structure of crarsm, an arsenic (III) S- adenosylmethionine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EVJ
- Type
- protein
- Length
- 607 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arsenite methyltransferase
- UniProt
- K0BVM7
- Ligands
- NA
- Pockets
- 8 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arsenite methyltransferase | protein | 306 | 30% helix, 26% strand | K0BVM7 |
| B | Arsenite methyltransferase | protein | 301 | 27% helix, 27% strand | K0BVM7 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 514 | 0.66 | 0.78 | 60 | empty |
| 2 | 71 | 0.62 | 0.91 | 24 | empty |
| 3 | 247 | 0.56 | 0.78 | 33 | empty |
| 4 | 292 | 0.53 | 0.75 | 37 | empty |
| 5 | 130 | 0.42 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 462 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5EVJ · X-ray crystal structure of CrArsM, an arsenic (III) S-adenosylmethionine… · 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 K0BVM7
- Elsewhere: RCSB PDB 5EVJ · PDBe 5EVJ · UniProt K0BVM7
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