Research workbench
Crystal structure of aminotransferase, class III from deinococcus radiodurans
Analyse Crystal structure of aminotransferase, class III from deinococcus radiodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3I4J
- Type
- protein
- Length
- 1,530 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminotransferase, class III
- UniProt
- Q9RZ32
- Ligands
- SO4
- Pockets
- 11 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Aminotransferase, class III | protein | 379 | 44% helix, 19% strand | Q9RZ32 |
| B, C | Aminotransferase, class III | protein | 386 | 44% helix, 18% strand | Q9RZ32 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.73 | 0.99 | 18 | empty |
| 2 | 56 | 0.72 | 0.99 | 18 | empty |
| 3 | 748 | 0.72 | 0.78 | 67 | empty |
| 4 | 56 | 0.71 | 0.98 | 17 | empty |
| 5 | 50 | 0.71 | 0.99 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 3524 Ų buried · 52 hydrogen bonds · protein-protein
- B–D · 3521 Ų buried · 54 hydrogen bonds · protein-protein
- A–D · 252 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3I4J · Crystal structure of Aminotransferase, class III from Deinococcus radiodurans · 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 Q9RZ32
- Elsewhere: RCSB PDB 3I4J · PDBe 3I4J · UniProt Q9RZ32
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