Research workbench
Crystal structure of serine acetyltransferase in complex with coenzyme a from brucella abortus strain S19
Analyse Crystal structure of serine acetyltransferase in complex with coenzyme a from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HZD
- Type
- protein
- Length
- 495 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyse, serine acetyltransferase
- UniProt
- B2S6A2
- Ligands
- COA, MG
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyse, serine acetyltransferase | protein | 250 | 44% helix, 17% strand | B2S6A2 |
| B | Cyse, serine acetyltransferase | protein | 245 | 44% helix, 17% strand | B2S6A2 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A, B
- 15P · Polyethylene glycol (N=34) · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.56 | 0.80 | 22 | empty |
| 2 | 89 | 0.39 | 0.77 | 15 | empty |
| 3 | 103 | 0.39 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 419 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4HZD · Crystal structure of Serine acetyltransferase in complex with Coenzyme A from Brucella… · 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 B2S6A2
- Elsewhere: RCSB PDB 4HZD · PDBe 4HZD · UniProt B2S6A2
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