Research workbench
Crystal structure of human branched chain amino acid aminotransferase (mitochondrial) complexed with pyridoxal-5'-phosphate at 2.5 ångströms (monoclinic form).
Analyse Crystal structure of human branched chain amino acid aminotransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EKP
- Type
- protein
- Length
- 730 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Branched chain amino acid aminotransferase (mitochondrial)
- EC
- 2.6.1.42
- UniProt
- O15382
- Ligands
- PLP
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Branched chain amino acid aminotransferase (mitochondrial) (EC 2.6.1.42) | protein | 365 | 24% helix, 30% strand | O15382 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 377 | 0.74 | 0.85 | 52 | PLP |
| 2 | 369 | 0.72 | 0.84 | 39 | PLP |
| 3 | 161 | 0.71 | 0.90 | 49 | empty |
| 4 | 139 | 0.68 | 0.89 | 24 | empty |
| 5 | 149 | 0.65 | 0.86 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 2412 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1EKP · Crystal structure of human branched chain amino acid aminotransferase (mitochondrial)… · the same entry in another collection · chain A against A, TM-score 1.00
- O15382 · AlphaFold monomer V2.0 prediction for branched-chain-amino-acid aminotransferase… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 O15382
- Elsewhere: RCSB PDB 1EKP · PDBe 1EKP · UniProt O15382
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