Research workbench
O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound
Analyse O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N2T
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q43317
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 309 | — | Q43317 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- CIT · Citric acid · additive · chains A
- 1PE · Pentaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7N2T · O-acetylserine sulfhydrylase from Citrullus vulgaris in the internal aldimine state, with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q43317 · AlphaFold monomer V2.0 prediction for cysteine synthase (Q43317) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q43317
- Elsewhere: RCSB PDB 7N2T · PDBe 7N2T · UniProt Q43317
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