Research workbench
Crystal structure of entamoeba histolytica serine acetyltransferase 1 in complex with L-cysteine
Analyse Crystal structure of entamoeba histolytica serine acetyltransferase 1 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P47
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine acetyltransferase
- EC
- 2.3.1.30
- UniProt
- Q9U8X2
- Ligands
- CYS, SO4
- Pockets
- 2 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine acetyltransferase (EC 2.3.1.30) | protein | 270 | 48% helix, 12% strand | Q9U8X2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.31 | 0.75 | 11 | empty |
| 2 | 52 | 0.29 | 0.76 | 17 | empty |
Compared structures
- 3P47 · Crystal structure of Entamoeba histolytica Serine acetyltransferase 1 in complex with… · 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 Q9U8X2
- Elsewhere: RCSB PDB 3P47 · PDBe 3P47 · UniProt Q9U8X2
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