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Crystal structure of T.TH HB8 glutamine aminotransferase complex with a-keto-G-methylthiobutyrate
Analyse Crystal structure of T.TH HB8 glutamine aminotransferase complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V2E
- Type
- protein
- Length
- 735 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine aminotransferase
- EC
- 2.6.1.15
- UniProt
- Q75WK2
- Ligands
- PLP, KMT
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine aminotransferase (EC 2.6.1.15) | protein | 368 | 42% helix, 17% strand | Q75WK2 |
| B | Glutamine aminotransferase (EC 2.6.1.15) | protein | 367 | 43% helix, 14% strand | Q75WK2 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- KMT · 4-(methylsulfanyl)-2-oxobutanoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.80 | 0.97 | 30 | PLP, KMT |
| 2 | 103 | 0.78 | 0.97 | 28 | PLP, KMT |
| 3 | 276 | 0.50 | 0.74 | 42 | empty |
| 4 | 176 | 0.45 | 0.74 | 19 | empty |
| 5 | 169 | 0.44 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 3186 Ų buried · 48 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1V2E · Crystal Structure of T.th HB8 Glutamine Aminotransferase complex with… · 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 Q75WK2
- Elsewhere: RCSB PDB 1V2E · PDBe 1V2E · UniProt Q75WK2
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