Research workbench
Crystal structure of homoserine O-acetyltransferase in complex with CoA from mycobacterium smegmatis atcc 19420
Analyse Crystal structure of homoserine O-acetyltransferase in complex with CoA from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IOI
- Type
- protein
- Length
- 740 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homoserine O-acetyltransferase
- EC
- 2.3.1.31
- UniProt
- A0A0D6HE46
- Ligands
- COA
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homoserine O-acetyltransferase (EC 2.3.1.31) | protein | 366 | 40% helix, 18% strand | A0A0D6HE46 |
| B | Homoserine O-acetyltransferase (EC 2.3.1.31) | protein | 374 | 39% helix, 18% strand | A0A0D6HE46 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.67 | 0.82 | 35 | empty |
| 2 | 327 | 0.66 | 0.81 | 44 | COA |
| 3 | 331 | 0.65 | 0.80 | 33 | COA |
| 4 | 180 | 0.54 | 0.79 | 38 | empty |
| 5 | 154 | 0.51 | 0.79 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 2037 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 6IOI · Crystal structure of Homoserine O-acetyltransferase in complex with CoA from… · 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 A0A0D6HE46
- Elsewhere: RCSB PDB 6IOI · PDBe 6IOI · UniProt A0A0D6HE46
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