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High resolution crystal structure of transketolase from campylobacter jejuni subsp. jejuni nctc 11168

Analyse High resolution crystal structure of transketolase from campylobacter jejuni… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3L84
Type: protein
Length: 632 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transketolase
EC: 2.2.1.1
UniProt: Q0P7Y3
Pockets: 5 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transketolase (EC 2.2.1.1)	protein	632	46% helix, 14% strand	Q0P7Y3

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A
ACT · Acetate ion · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	130	0.61	0.85	24	empty
2	180	0.48	0.76	20	empty
3	202	0.47	0.74	34	empty
4	67	0.42	0.81	16	GOL
5	61	0.28	0.74	13	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

3L84 · High resolution crystal structure of transketolase from Campylobacter jejuni subsp.… · 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 Q0P7Y3
Elsewhere: RCSB PDB 3L84 · PDBe 3L84 · UniProt Q0P7Y3

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