Research workbench
Human branched chain amino acid aminotransferase : three dimensional structure of the enzyme in its pyridoxamine phosphate form.
Analyse Human branched chain amino acid aminotransferase : three dimensional structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KTA
- 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
- PMP, KIV
- Pockets
- 4 · best druggability 0.80
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
- PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- KIV · 3-methyl-2-oxobutanoic acid · ligand · chains A, B
- ACY · Acetic acid · additive · 7 copies · chains A, B
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 825 | 0.80 | 0.83 | 79 | PMP, KIV |
| 2 | 678 | 0.78 | 0.83 | 71 | PMP |
| 3 | 141 | 0.71 | 0.91 | 44 | empty |
| 4 | 71 | 0.32 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2401 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 1KTA · Human branched chain amino acid aminotransferase : three dimensional structure of the… · 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 1KTA · PDBe 1KTA · UniProt O15382
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