Research workbench
Crystal structure of maltose O-acetyltransferase complexed with acetyl coenzyme a from bacillus anthracis
Analyse Crystal structure of maltose O-acetyltransferase complexed with acetyl coenzyme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IGJ
- Type
- protein
- Length
- 561 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose O-acetyltransferase
- EC
- 2.3.1.79
- UniProt
- Q81N16
- Ligands
- ACO, SO4
- Pockets
- 5 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 22% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose O-acetyltransferase (EC 2.3.1.79) | protein | 186 | 23% helix, 28% strand | Q81N16 |
| B | Maltose O-acetyltransferase (EC 2.3.1.79) | protein | 187 | 22% helix, 29% strand | Q81N16 |
| C | Maltose O-acetyltransferase (EC 2.3.1.79) | protein | 188 | 21% helix, 28% strand | Q81N16 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 3 copies · chains A, C, B
- SO4 · Sulfate ion · ion · 6 copies · chains A, B, C
- FMT · Formic acid · additive · 7 copies · chains A, B, C
- GOL · Glycerol · additive · 3 copies · chains A, C
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 | 276 | 0.85 | 0.96 | 44 | empty |
| 2 | 580 | 0.76 | 0.83 | 68 | ACO, SO4 |
| 3 | 555 | 0.75 | 0.82 | 65 | ACO, GOL |
| 4 | 535 | 0.73 | 0.82 | 69 | ACO, SO4 |
| 5 | 134 | 0.66 | 0.89 | 19 | SO4 |
Interfaces
3 interfaces between chains.
- A–B · 1307 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 1302 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1247 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 modified (engineered).
Compared structures
- 3IGJ · Crystal Structure of Maltose O-acetyltransferase Complexed with Acetyl Coenzyme A 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 Q81N16
- Elsewhere: RCSB PDB 3IGJ · PDBe 3IGJ · UniProt Q81N16
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