Research workbench
Crystal structure of eschelichia COLI branched-chain amino acid aminotransferase.
Analyse Crystal structure of eschelichia COLI branched-chain amino acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I1K
- Type
- protein
- Length
- 894 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Branched-chain amino acid aminotransferase
- EC
- 2.6.1.42
- UniProt
- P0AB80
- Ligands
- PLP
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Branched-chain amino acid aminotransferase (EC 2.6.1.42) | protein | 298 | 30% helix, 27% strand | P0AB80 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 686 | 0.80 | 0.84 | 58 | empty |
| 2 | 372 | 0.72 | 0.84 | 42 | empty |
| 3 | 421 | 0.72 | 0.83 | 42 | empty |
| 4 | 197 | 0.64 | 0.84 | 38 | PLP |
| 5 | 214 | 0.64 | 0.83 | 43 | PLP |
Interfaces
3 interfaces between chains.
- A–C · 654 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 652 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 647 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1I1K · Crystal structure of eschelichia COLI branched-chain amino acid aminotransferase. · the same entry in another collection · chain A against A, TM-score 1.00
- P0AB80 · AlphaFold monomer V2.0 prediction for branched-chain-amino-acid aminotransferase (P0AB80) · a predicted model of the same protein · chain A 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 P0AB80
- Elsewhere: RCSB PDB 1I1K · PDBe 1I1K · UniProt P0AB80
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