Research workbench
Crystal structure of maltose transacetylase from geobacillus kaustophilus P2(1) crystal form
Analyse Crystal structure of maltose transacetylase from geobacillus kaustophilus P2(1)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P2O
- Type
- protein
- Length
- 1,103 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose transacetylase
- EC
- 2.3.1.79
- UniProt
- Q75TD0
- Pockets
- 10 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, F | Maltose transacetylase (EC 2.3.1.79) | protein | 184 | 23% helix, 30% strand | Q75TD0 |
| D | Maltose transacetylase (EC 2.3.1.79) | protein | 183 | 23% helix, 31% strand | Q75TD0 |
Pockets
10 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1066 | 0.82 | 0.83 | 106 | empty |
| 2 | 482 | 0.77 | 0.85 | 46 | empty |
| 3 | 92 | 0.77 | 0.99 | 20 | empty |
| 4 | 545 | 0.75 | 0.83 | 67 | empty |
| 5 | 442 | 0.75 | 0.84 | 56 | empty |
Interfaces
9 interfaces between chains.
- A–B · 1321 Ų buried · 20 hydrogen bonds · protein-protein
- D–E · 1274 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 1243 Ų buried · 15 hydrogen bonds · protein-protein
- D–F · 1235 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 1226 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2P2O · Crystal structure of maltose transacetylase from Geobacillus kaustophilus P2(1) crystal… · 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 Q75TD0
- Elsewhere: RCSB PDB 2P2O · PDBe 2P2O · UniProt Q75TD0
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