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Crystals structure of a bacillus anthracis aminotransferase
Analyse Crystals structure of a bacillus anthracis aminotransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3N5M
- Type
- protein
- Length
- 1,805 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- UniProt
- Q6I0U5
- Ligands
- SO4, CL
- Pockets
- 18 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Adenosylmethionine-8-amino-7-oxononanoate aminotransferase | protein | 452 | 41% helix, 18% strand | Q6I0U5 |
| B | Adenosylmethionine-8-amino-7-oxononanoate aminotransferase | protein | 450 | 40% helix, 18% strand | Q6I0U5 |
| D | Adenosylmethionine-8-amino-7-oxononanoate aminotransferase | protein | 451 | 39% helix, 18% strand | Q6I0U5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 8 copies · chains A, D, B, C
- CL · Chloride ion · ion · 8 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 734 | 0.80 | 0.84 | 67 | SO4 |
| 2 | 720 | 0.80 | 0.84 | 65 | SO4 |
| 3 | 723 | 0.80 | 0.84 | 65 | SO4 |
| 4 | 729 | 0.80 | 0.84 | 64 | SO4 |
| 5 | 146 | 0.80 | 0.97 | 30 | empty |
Interfaces
6 interfaces between chains.
- B–C · 5634 Ų buried · 68 hydrogen bonds · protein-protein
- A–D · 5610 Ų buried · 67 hydrogen bonds · protein-protein
- C–D · 1361 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1361 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 234 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 68 modified (engineered).
Compared structures
- 3N5M · Crystals structure of a Bacillus anthracis aminotransferase · 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 Q6I0U5
- Elsewhere: RCSB PDB 3N5M · PDBe 3N5M · UniProt Q6I0U5
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