Research workbench
Lysine aminotransferase from M. tuberculosis in external aldimine form
Analyse Lysine aminotransferase from M. tuberculosis in external aldimine form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CJD
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-lysine-epsilon aminotransferase
- EC
- 2.6.1.36
- UniProt
- P63509
- Ligands
- LYS, PLP
- Pockets
- 5 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-lysine-epsilon aminotransferase (EC 2.6.1.36) | protein | 435 | 43% helix, 16% strand | P63509 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.46 | 0.77 | 19 | empty |
| 2 | 154 | 0.45 | 0.76 | 21 | empty |
| 3 | 76 | 0.44 | 0.81 | 20 | LYS, PLP |
| 4 | 153 | 0.40 | 0.73 | 39 | empty |
| 5 | 60 | 0.28 | 0.73 | 15 | empty |
Compared structures
- 2CJD · Lysine aminotransferase from M. tuberculosis in external aldimine form · the same entry in another collection · chain A 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 P63509
- Elsewhere: RCSB PDB 2CJD · PDBe 2CJD · UniProt P63509
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