Research workbench
Crystal structure of maltose O-acetyltransferase from bacillus anthracis
Analyse Crystal structure of maltose O-acetyltransferase from bacillus anthracis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HJJ
- Type
- protein
- Length
- 562 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
- SO4
- Pockets
- 5 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 22% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose O-acetyltransferase (EC 2.3.1.79) | protein | 189 | 22% helix, 28% strand | Q81N16 |
| B | Maltose O-acetyltransferase (EC 2.3.1.79) | protein | 187 | 22% helix, 28% strand | Q81N16 |
| C | Maltose O-acetyltransferase (EC 2.3.1.79) | protein | 186 | 23% helix, 28% strand | Q81N16 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 9 copies · chains A, C, B
- ACY · Acetic acid · additive · 6 copies · chains A, C, 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 | 296 | 0.84 | 0.95 | 42 | empty |
| 2 | 545 | 0.73 | 0.81 | 68 | ACY, GOL |
| 3 | 551 | 0.72 | 0.81 | 69 | ACY, GOL |
| 4 | 521 | 0.71 | 0.81 | 66 | ACY, GOL |
| 5 | 109 | 0.67 | 0.91 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1315 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 1269 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 1231 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3HJJ · Crystal Structure of Maltose O-acetyltransferase from Bacillus anthracis · 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 3HJJ · PDBe 3HJJ · UniProt Q81N16
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