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As (III) S-adenosylmethyltransferase cysteine mutant C72A bound phenylarsine oxide (PHAS(III) in the arsenic binding site
Analyse As (III) S-adenosylmethyltransferase cysteine mutant C72A bound phenylarsine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EG5
- Type
- protein
- Length
- 322 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arsenic methyltransferase
- UniProt
- C0JV69
- Ligands
- PA0, CA
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arsenic methyltransferase | protein | 322 | 34% helix, 24% strand | C0JV69 |
Ligands and binding sites
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 | 165 | 0.54 | 0.80 | 26 | CA |
| 2 | 88 | 0.46 | 0.81 | 19 | empty |
| 3 | 101 | 0.36 | 0.74 | 27 | empty |
Compared structures
- 5EG5 · As (III) S-adenosylmethyltransferase cysteine mutant C72A bound Phenylarsine oxide… · 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 5EG5 · PDBe 5EG5 · UniProt C0JV69
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