MolNFT v1 · #142847 · protein
Crystal structure of O-acetylserine dependent cystathionine beta- synthase from helicobacter pylori.
6AHI · Cysteine synthase: “Crystal structure of O-acetylserine dependent cystathionine beta- synthase from helicobacter pylori.”. X-ray diffraction, 1 ligand (MET), 7 pockets (best druggability 0.77). MolNFT v1 #142847 on GenesisL1: 3D…
- PDB
- 6AHI
- Type
- protein
- Length
- 612 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase
- EC
- 2.5.1.47
- UniProt
- P56067
- Ligands
- MET
- Pockets
- 7 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cysteine synthase (EC 2.5.1.47) | protein | 306 | 42% helix, 19% strand | P56067 |
Ligands and binding sites
- MET · Methionine · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.77 | 0.96 | 24 | empty |
| 2 | 181 | 0.69 | 0.87 | 26 | empty |
| 3 | 399 | 0.68 | 0.81 | 41 | empty |
| 4 | 192 | 0.63 | 0.83 | 34 | MET |
| 5 | 126 | 0.42 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1825 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 6AHI · Crystal structure of O-acetylserine dependent cystathionine beta-synthase from… · the same entry in another collection · chain A against A, TM-score 1.00
- P56067 · AlphaFold monomer V2.0 prediction for cysteine synthase (P56067) · a predicted model of the same protein · 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 P56067
- Elsewhere: RCSB PDB 6AHI · PDBe 6AHI · UniProt P56067
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