Research workbench
1.6 ångström resolution crystal structure of putative streptothricin acetyltransferase from bacillus anthracis str. ames in complex with acetyl coenzyme a
Analyse 1.6 ångström resolution crystal structure of putative streptothricin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PP9
- Type
- protein
- Length
- 523 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative streptothricin acetyltransferase
- UniProt
- Q81NK7
- Ligands
- ACO, K, PO4
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 22% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative streptothricin acetyltransferase | protein | 176 | 22% helix, 43% strand | Q81NK7 |
| B | Putative streptothricin acetyltransferase | protein | 174 | 22% helix, 41% strand | Q81NK7 |
| C | Putative streptothricin acetyltransferase | protein | 173 | 23% helix, 43% strand | Q81NK7 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 3 copies · chains A, B, C
- K · Potassium ion · metal · 2 copies · chains A, C
- PO4 · Phosphate ion · ion · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 406 | 0.69 | 0.81 | 38 | PO4, K |
| 2 | 246 | 0.68 | 0.84 | 29 | ACO |
| 3 | 224 | 0.67 | 0.84 | 26 | ACO |
| 4 | 323 | 0.62 | 0.78 | 31 | ACO |
| 5 | 148 | 0.42 | 0.74 | 30 | empty |
Interfaces
2 interfaces between chains.
- B–C · 1103 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 124 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 3PP9 · 1.6 Angstrom resolution crystal structure of putative streptothricin acetyltransferase… · 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 Q81NK7
- Elsewhere: RCSB PDB 3PP9 · PDBe 3PP9 · UniProt Q81NK7
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