MolNFT v1 · #101530 · protein
Crystal structure of O-acetylserine sulfhydrylase from haemophilus influenzae in complex with high affinity inhibitory peptide from serine acetyl transferase of salmonella typhimurium at 2.0 a
4NU8 · Cysteine synthase: “Crystal structure of O-acetylserine sulfhydrylase from haemophilus influenzae in complex with high affinity…”. X-ray diffraction, 2 pockets (best druggability 0.46). MolNFT v1 #101530 on GenesisL1: 3D structure…
- PDB
- 4NU8
- Type
- protein
- Length
- 319 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase; Peptide from serine acetyltransferase
- EC
- 2.5.1.47
- UniProt
- P45040, Q8Z2E9
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Cysteine synthase (EC 2.5.1.47) | protein | 311 | 43% helix, 17% strand | P45040 |
| A | Peptide from serine acetyltransferase | protein | 8 | 0% helix, 13% strand | Q8Z2E9 |
Ligands and binding sites
- GOL · Glycerol · additive · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.46 | 0.76 | 35 | empty |
| 2 | 69 | 0.41 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- X–A · 630 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- 4NU8 · Crystal structure of O-acetylserine sulfhydrylase from Haemophilus influenzae in complex… · the same entry in another collection · chain X against X, TM-score 1.00
- P45040 · AlphaFold monomer V2.0 prediction for cysteine synthase (P45040) · a predicted model of the same protein · chain X 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 P45040
- Every structure of UniProt Q8Z2E9
- Elsewhere: RCSB PDB 4NU8 · PDBe 4NU8 · UniProt P45040 · UniProt Q8Z2E9
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