Research workbench
The structure of gamma-aminobutyrate aminotransferase mutant: I50Q
Analyse The structure of gamma-aminobutyrate aminotransferase mutant: I50Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SZS
- Type
- protein
- Length
- 1,700 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-aminobutyrate aminotransferase
- EC
- 2.6.1.19
- UniProt
- P22256
- Ligands
- PLP, PMP, SO4
- Pockets
- 16 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | 4-aminobutyrate aminotransferase (EC 2.6.1.19) | protein | 425 | 42% helix, 20% strand | P22256 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D
- PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 15 copies · chains A, C, B, D
- EDO · 1,2-ethanediol · additive · 17 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.80 | 0.95 | 41 | EDO |
| 2 | 174 | 0.79 | 0.95 | 43 | EDO |
| 3 | 496 | 0.79 | 0.86 | 67 | empty |
| 4 | 379 | 0.76 | 0.86 | 56 | EDO, PLP, PMP, SO4 |
| 5 | 339 | 0.73 | 0.85 | 55 | SO4, EDO, PLP, PMP |
Interfaces
6 interfaces between chains.
- A–B · 4698 Ų buried · 91 hydrogen bonds · protein-protein
- C–D · 4690 Ų buried · 91 hydrogen bonds · protein-protein
- B–D · 1194 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 1193 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 50 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor, 1 covalent (pyridoxal phosphate Schiff base, covalent ligand).
Compared structures
- 1SZS · The structure of gamma-aminobutyrate aminotransferase mutant: I50Q · the same entry in another collection · chain B against B, TM-score 1.00
- P22256 · AlphaFold monomer V2.0 prediction for 4-aminobutyrate aminotransferase gabt (P22256) · a predicted model of the same protein · chain C 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 P22256
- Elsewhere: RCSB PDB 1SZS · PDBe 1SZS · UniProt P22256
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