Research workbench
Crystal structure of O-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
Analyse Crystal structure of O-acetylserine sulfhydrylase with bound transcription… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XOQ
- Type
- protein
- Length
- 636 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase; Gly-phe-ser-gly-gly-asp-gly-ile
- EC
- 2.5.1.47
- UniProt
- D5STP0
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cysteine synthase (EC 2.5.1.47) | protein | 310 | 43% helix, 18% strand | D5STP0 |
| C, D | Gly-phe-ser-gly-gly-asp-gly-ile | protein | 8 | 0% helix, 13% strand | — |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.62 | 0.79 | 53 | empty |
| 2 | 156 | 0.52 | 0.79 | 30 | empty |
| 3 | 81 | 0.45 | 0.80 | 14 | empty |
| 4 | 85 | 0.42 | 0.79 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2594 Ų buried · 43 hydrogen bonds · protein-protein
- A–C · 606 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 578 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 5XOQ · Crystal structure of O-Acetylserine Sulfhydrylase with bound Transcription Factor peptide… · 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 D5STP0
- Elsewhere: RCSB PDB 5XOQ · PDBe 5XOQ · UniProt D5STP0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.