MolNFT v1 · #69373 · protein

Crystal structure of apo transketolase from francisella tularensis

3KOM: “Crystal structure of apo transketolase from francisella tularensis”. X-ray diffraction, 17 pockets (best druggability 0.74). MolNFT v1 #69373 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3KOM
Type: protein
Length: 1,302 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transketolase
EC: 2.2.1.1
UniProt: Q5NF74
Pockets: 17 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transketolase (EC 2.2.1.1)	protein	654	44% helix, 13% strand	Q5NF74
B	Transketolase (EC 2.2.1.1)	protein	648	44% helix, 13% strand	Q5NF74

Pockets

17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	354	0.74	0.85	49	empty
2	483	0.68	0.79	56	empty
3	229	0.62	0.81	42	empty
4	230	0.58	0.80	36	empty
5	185	0.51	0.77	26	empty

Interfaces

1 interface between chains.

A–B · 3952 Å² buried · 59 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 42 modified (engineered, oxidation).

Compared structures

3KOM · Crystal structure of apo transketolase from Francisella tularensis · 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 Q5NF74
Elsewhere: RCSB PDB 3KOM · PDBe 3KOM · UniProt Q5NF74

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