Research workbench
Crystal structure of T.TH. HB8 O-acetylserine sulfhydrylase
Analyse Crystal structure of T.TH. HB8 O-acetylserine sulfhydrylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VE1
- Type
- protein
- Length
- 302 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
- Q5SLE6
- Ligands
- PLP
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-acetylserine sulfhydrylase (EC 2.5.1.47) | protein | 302 | 42% helix, 18% strand | Q5SLE6 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 589 | 0.71 | 0.79 | 52 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1VE1 · Crystal Structure of T.th. HB8 O-acetylserine sulfhydrylase · 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 Q5SLE6
- Elsewhere: RCSB PDB 1VE1 · PDBe 1VE1 · UniProt Q5SLE6
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