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Structure of the mycobacterium tuberculosis O-acetylserine sulfhydrylase (oass) CYSK1 in complex with a small molecule inhibitor
Analyse Structure of the mycobacterium tuberculosis O-acetylserine sulfhydrylase (oass)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZEI
- Type
- protein
- Length
- 300 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- O-acetylserine sulfhydrylase
- EC
- 2.5.1.47
- UniProt
- P0A534
- Ligands
- PLP, AWH
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-acetylserine sulfhydrylase (EC 2.5.1.47) | protein | 300 | 43% helix, 18% strand | P0A534 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
- AWH · 3-[(Z)-[(5Z)-5-[[2-(2-hydroxy-2-oxoethyloxy)phenyl]methylidene]-3-methyl-4-oxidanylidene-1,3-thiazolidin-2-ylidene]amino]benzoic acid · ligand · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 422 | 0.70 | 0.81 | 55 | PLP, AWH |
| 2 | 53 | 0.30 | 0.75 | 11 | MPD |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 3ZEI · Structure of the Mycobacterium tuberculosis O-Acetylserine Sulfhydrylase (OASS) CysK1 in… · 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 P0A534
- Elsewhere: RCSB PDB 3ZEI · PDBe 3ZEI · UniProt P0A534
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