Research workbench
Crystal structure of O-acetyl homoserine sulfhydrylase from thermus thermophilus HB8
Analyse Crystal structure of O-acetyl homoserine sulfhydrylase from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CTZ
- Type
- protein
- Length
- 842 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- O-acetyl-L-homoserine sulfhydrylase
- EC
- 2.5.1.-
- UniProt
- Q93I77
- Ligands
- PLP
- Pockets
- 11 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | O-acetyl-L-homoserine sulfhydrylase (EC 2.5.1.-) | protein | 421 | 44% helix, 15% strand | Q93I77 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.66 | 0.81 | 51 | PLP |
| 2 | 252 | 0.66 | 0.83 | 42 | PLP |
| 3 | 87 | 0.52 | 0.84 | 21 | empty |
| 4 | 95 | 0.46 | 0.80 | 21 | empty |
| 5 | 69 | 0.46 | 0.83 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 974 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 2CTZ · Crystal structure of o-acetyl homoserine sulfhydrylase from Thermus thermophilus HB8 · 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 Q93I77
- Elsewhere: RCSB PDB 2CTZ · PDBe 2CTZ · UniProt Q93I77
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