Research workbench
Crystal structure of O-acetylserine sulfhydrylase B
Analyse Crystal structure of O-acetylserine sulfhydrylase B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BHT
- Type
- protein
- Length
- 1,152 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase B
- EC
- 2.5.1.47
- UniProt
- P16703
- Ligands
- PLP
- Pockets
- 19 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine synthase B (EC 2.5.1.47) | protein | 294 | 43% helix, 17% strand | P16703 |
| B | Cysteine synthase B (EC 2.5.1.47) | protein | 281 | 36% helix, 16% strand | P16703 |
| C | Cysteine synthase B (EC 2.5.1.47) | protein | 292 | 40% helix, 19% strand | P16703 |
| D | Cysteine synthase B (EC 2.5.1.47) | protein | 285 | 38% helix, 15% strand | P16703 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 790 | 0.82 | 0.85 | 85 | PLP |
| 2 | 860 | 0.77 | 0.81 | 76 | PLP |
| 3 | 658 | 0.75 | 0.81 | 73 | empty |
| 4 | 94 | 0.75 | 0.97 | 33 | PLP |
| 5 | 69 | 0.72 | 0.98 | 27 | PLP |
Interfaces
5 interfaces between chains.
- C–D · 1633 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1563 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 605 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 439 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 39 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 cofactor (pyridoxal phosphate Schiff base).
Compared structures
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 P16703
- Elsewhere: RCSB PDB 2BHT · PDBe 2BHT · UniProt P16703
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.