Research workbench
Human branched chain amino acid aminotransferase (mitochondrial): three dimensional structure of enzyme inactivated by tris bound to the pyridoxal-5'-phosphate on one end and active site LYS202 nz on the other.
Analyse Human branched chain amino acid aminotransferase (mitochondrial): three… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EKV
- 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 0.76
Structure
x-ray diffraction · 1 distinct chain · 25% 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 | 25% helix, 29% strand | O15382 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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 | 119 | 0.76 | 0.95 | 42 | empty |
| 2 | 431 | 0.75 | 0.84 | 46 | PLP, TRS |
| 3 | 439 | 0.73 | 0.83 | 46 | PLP, TRS |
| 4 | 107 | 0.69 | 0.91 | 21 | empty |
| 5 | 121 | 0.67 | 0.89 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 2377 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 1EKV · Human branched chain amino acid aminotransferase (mitochondrial): three dimensional… · 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 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 O15382
- Elsewhere: RCSB PDB 1EKV · PDBe 1EKV · UniProt O15382
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