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Lysine aminotransferase from M. tuberculosis in the internal aldimine form with bound substrate 2-ketoglutarate

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

PDB: 2CJH
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, AKG
Pockets: 5 · best druggability 0.45

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
AKG · 2-oxoglutaric acid · ligand · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	134	0.45	0.76	19	empty
2	142	0.45	0.76	20	empty
3	92	0.42	0.78	23	PLP, AKG
4	73	0.31	0.74	23	empty
5	54	0.26	0.72	15	empty

Compared structures

2CJH · Lysine aminotransferase from M. tuberculosis in the internal aldimine form with bound… · 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 2CJH · PDBe 2CJH · UniProt P63509

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