Research workbench
Crystal structure of O-acetyl-serine sulfhydrylase from entamoeba histolytica in complex with cysteine
Analyse Crystal structure of O-acetyl-serine sulfhydrylase from entamoeba histolytica… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BM5
- Type
- protein
- Length
- 673 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase
- UniProt
- O15570
- Ligands
- PLP, CYS, SO4
- Pockets
- 10 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine synthase | protein | 338 | 43% helix, 17% strand | O15570 |
| B | Cysteine synthase | protein | 335 | 41% helix, 17% strand | O15570 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- CYS · Cysteine · ligand · chains B
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.73 | 0.97 | 28 | PLP |
| 2 | 424 | 0.70 | 0.81 | 55 | PLP, SO4 |
| 3 | 152 | 0.63 | 0.86 | 33 | CYS |
| 4 | 137 | 0.53 | 0.81 | 19 | empty |
| 5 | 113 | 0.43 | 0.78 | 16 | SO4 |
Interfaces
1 interface between chains.
- A–B · 2997 Ų buried · 32 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 3BM5 · Crystal structure of O-acetyl-serine sulfhydrylase from Entamoeba histolytica in complex… · 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 O15570
- Elsewhere: RCSB PDB 3BM5 · PDBe 3BM5 · UniProt O15570
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