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Crystal structure of O-acetyl serine sulfhydrylase from entamoeba histolytica in complex with isoleucine
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
- 4IL5
- Type
- protein
- Length
- 670 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase
- EC
- 2.5.1.47
- UniProt
- O15570
- Ligands
- ILE, SO4
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine synthase (EC 2.5.1.47) | protein | 336 | 43% helix, 18% strand | O15570 |
| B | Cysteine synthase (EC 2.5.1.47) | protein | 334 | 42% helix, 17% strand | O15570 |
Ligands and binding sites
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 | 421 | 0.65 | 0.79 | 37 | ILE |
| 2 | 409 | 0.64 | 0.78 | 38 | SO4 |
| 3 | 115 | 0.54 | 0.83 | 21 | empty |
| 4 | 77 | 0.52 | 0.85 | 18 | empty |
| 5 | 127 | 0.49 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 3109 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 4IL5 · 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 4IL5 · PDBe 4IL5 · UniProt O15570
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