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Lysine aminotransferase from M. tuberculosis in the internal aldimine form

Analyse Lysine aminotransferase from M. tuberculosis in the internal aldimine form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CIN
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: PLP
Pockets: 3 · best druggability 0.44

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

PLP · Pyridoxal-5'-phosphate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.44	0.77	19	empty
2	139	0.43	0.75	18	empty
3	111	0.35	0.74	29	empty

Modifications

Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).

Compared structures

2CIN · Lysine aminotransferase from M. tuberculosis in the internal 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 2CIN · PDBe 2CIN · UniProt P63509

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