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Cyrstal structure of O-acetylserine sulfhydrylase ternary complex from haemophilus influenzae at 2.2 a
Analyse Cyrstal structure of O-acetylserine sulfhydrylase ternary complex from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ORE
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase; Peptide inhibitor
- EC
- 2.5.1.47
- UniProt
- P45040
- Ligands
- OAS
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Cysteine synthase (EC 2.5.1.47) | protein | 308 | 41% helix, 17% strand | P45040 |
| A | Peptide inhibitor | protein | 8 | 0% helix, 13% strand | — |
Ligands and binding sites
- OAS · O-acetylserine · ligand · chains X, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.56 | 0.89 | 22 | empty |
| 2 | 54 | 0.36 | 0.79 | 13 | empty |
Interfaces
1 interface between chains.
- X–A · 645 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- 4ORE · Cyrstal structure of O-acetylserine sulfhydrylase ternary complex from Haemophilus… · the same entry in another collection · chain A against A, 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 0.99
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
- Elsewhere: RCSB PDB 4ORE · PDBe 4ORE · UniProt P45040
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