Research workbench
Crystal structure of putative aminotransferase (AAH25799.1) from mus musculus at 1.80 a resolution
Analyse Crystal structure of putative aminotransferase (AAH25799.1) from mus musculus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KGX
- Type
- protein
- Length
- 773 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alanine-glyoxylate aminotransferase
- UniProt
- Q8R128
- Ligands
- MG, CL
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alanine-glyoxylate aminotransferase | protein | 383 | 41% helix, 16% strand | Q8R128 |
| B | Alanine-glyoxylate aminotransferase | protein | 390 | 41% helix, 15% strand | Q8R128 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 9 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.84 | 0.88 | 81 | EDO |
| 2 | 533 | 0.74 | 0.82 | 50 | empty |
| 3 | 61 | 0.52 | 0.86 | 15 | empty |
| 4 | 209 | 0.49 | 0.76 | 25 | EDO |
| 5 | 80 | 0.40 | 0.78 | 26 | EDO |
Interfaces
1 interface between chains.
- A–B · 4439 Ų buried · 57 hydrogen bonds · protein-protein
Compared structures
- 3KGX · Crystal structure of Putative aminotransferase (AAH25799.1) from MUS MUSCULUS at 1.80 A… · 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 Q8R128
- Elsewhere: RCSB PDB 3KGX · PDBe 3KGX · UniProt Q8R128
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