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Crystallographic structure of human branched chain amino acid aminotransferase (mitochondrial) complexed with pyridoxal-5'- phosphate at 1.95 ångströms (orthorhombic form)
Analyse Crystallographic 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
- 1EKF
- 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
- 5 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Branched chain amino acid aminotransferase (mitochondrial) (EC 2.6.1.42) | protein | 365 | 23% helix, 29% 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
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 737 | 0.81 | 0.84 | 79 | PLP |
| 2 | 400 | 0.72 | 0.83 | 45 | PLP |
| 3 | 152 | 0.70 | 0.89 | 48 | empty |
| 4 | 197 | 0.66 | 0.85 | 27 | empty |
| 5 | 96 | 0.36 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2362 Ų buried · 35 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1EKF · Crystallographic structure of human branched chain amino acid aminotransferase… · the same entry in another collection · chain B against B, 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 1EKF · PDBe 1EKF · UniProt O15382
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