Research workbench
Crystal structure of human branched chain amino acid transaminase in a complex with an inhibitor, C16H10N2O4F3SCL, and pyridoxal 5' phosphate.
Analyse Crystal structure of human branched chain amino acid transaminase in a complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ABJ
- Type
- protein
- Length
- 1,449 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Branched-chain-amino-acid aminotransferase, cytosolic
- EC
- 2.6.1.42
- UniProt
- P54687
- Ligands
- CBC, PLP
- Pockets
- 14 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 26% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, J | Branched-chain-amino-acid aminotransferase, cytosolic (EC 2.6.1.42) | protein | 366 | 26% helix, 31% strand | P54687 |
| D | Branched-chain-amino-acid aminotransferase, cytosolic (EC 2.6.1.42) | protein | 359 | 26% helix, 31% strand | P54687 |
| G | Branched-chain-amino-acid aminotransferase, cytosolic (EC 2.6.1.42) | protein | 358 | 26% helix, 31% strand | P54687 |
Ligands and binding sites
- CBC · N'-(5-chlorobenzofuran-2-carbonyl)-2-(trifluoromethyl) benzenesulfonohydrazide · ligand · 4 copies · chains A, D, G, J
- PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, D, G, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 395 | 0.75 | 0.85 | 46 | CBC, PLP |
| 2 | 935 | 0.75 | 0.78 | 69 | empty |
| 3 | 506 | 0.74 | 0.82 | 59 | CBC, PLP |
| 4 | 488 | 0.74 | 0.82 | 55 | CBC, PLP |
| 5 | 399 | 0.72 | 0.83 | 51 | CBC, PLP |
Interfaces
4 interfaces between chains.
- G–J · 2431 Ų buried · 34 hydrogen bonds · protein-protein
- A–D · 2415 Ų buried · 34 hydrogen bonds · protein-protein
- A–G · 503 Ų buried · 3 hydrogen bonds · protein-protein
- A–J · 57 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 2ABJ · Crystal structure of human branched chain amino acid transaminase in a complex with an… · the same entry in another collection · chain J against J, TM-score 1.00
- P54687 · AlphaFold monomer V2.0 prediction for branched-chain-amino-acid aminotransferase… · a predicted model of the same protein · chain G 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 P54687
- Elsewhere: RCSB PDB 2ABJ · PDBe 2ABJ · UniProt P54687
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