Proteins

Genome: KpATCC43816

Description: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome

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9 proteins

Scoring formula None

Sorted by Druggability (descending)

Applied filters EC Number: 4.2.1.3

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EC Number: 4.2.1.3 ×
# Protein Description Gene Structure EC GO Druggability FPocket druggability score for the preferred structure (0–1): experimental structure when available, otherwise predicted model. ≥ 0.7 highly druggable · ≥ 0.4 moderately druggable · < 0.4 low druggability. Human off-target BLASTP against the human proteome. Hit means at least one human match was detected at e-value <= 1e-5. Prefer No hit for pathogen-selective targets. Human identity (%) Best human BLAST identity percentage. Human E-value Best human BLAST E-value.
1 VK055_3984 glycerol dehydratase large subunit dhaB4 Experimental + ColabFold
4.2.1.30
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0046405Catalysis of the reaction: glycerol = 3-hydroxypropanal + H2O. GO:0046872Binding to a metal ion.
0.938 No Hit 0.0% —
2 VK055_3982 glycerol dehydrase beta subunit gldB Experimental + ColabFold
4.2.1.30 4.2.1.28
GO:0046405Catalysis of the reaction: glycerol = 3-hydroxypropanal + H2O. GO:0050215Catalysis of the reaction: propane-1,2-diol = H2O + propanal.
0.803 No Hit 0.0% —
3 VK055_3981 glycerol dehydratase large subunit dhaB Experimental + ColabFold
4.2.1.30
GO:0031419Binding to cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. GO:0003824Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0016836Catalysis of the cleavage of a carbon-oxygen bond by elimination of water. +14 total
0.699 No Hit 0.0% —
4 VK055_3983 glycerol dehydrase gamma subunit dhaB3 Experimental + ColabFold
4.2.1.30 4.2.1.28
GO:0046405Catalysis of the reaction: glycerol = 3-hydroxypropanal + H2O. GO:0050215Catalysis of the reaction: propane-1,2-diol = H2O + propanal.
0.695 No Hit 0.0% —
5 VK055_3838 L-tartrate dehydratase, beta subunit ttdB AlphaFold + ColabFold
4.2.1.32
GO:0016836Catalysis of the cleavage of a carbon-oxygen bond by elimination of water. GO:0008730Catalysis of the reaction: L-tartrate = H2O + oxaloacetate.
0.621 No Hit 0.0% —
6 VK055_3837 L-tartrate dehydratase, &alpha subunit AlphaFold + ColabFold
4.2.1.32
GO:0016829Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. GO:0051539Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0008730Catalysis of the reaction: L-tartrate = H2O + oxaloacetate. +14 total
0.34 No Hit 0.0% —
7 VK055_2496 leuD leuD AlphaFold + ColabFold
4.2.1.33
GO:0009316A heterodimeric enzyme complex composed of subunits leuC and leuD. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. GO:0009098The chemical reactions and pathways resulting in the formation of L-leucine, 2-amino-4-methylpentanoic acid. GO:0003861Catalysis of the reaction: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. +14 total
0.335 No Hit 0.0% —
8 VK055_2445 aconitate hydratase 2 acnB AlphaFold + ColabFold
4.2.1.3 4.2.1.99
GO:0006099A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. GO:0051539Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0003994Catalysis of the reaction: citrate = isocitrate. The reaction occurs in two steps: (1) citrate = cis-aconitate + H2O, (2) cis-aconitate + H2O = isocitrate. This reaction is the interconversion of citrate and isocitrate via the labile, enzyme-bound intermediate cis-aconitate. Water is removed from one part of the citrate molecule and added back to a different atom to form isocitrate. +58 total
0.217 No Hit 0.0% —
9 VK055_2495 leuC leuC AlphaFold + ColabFold
4.2.1.33
GO:0009098The chemical reactions and pathways resulting in the formation of L-leucine, 2-amino-4-methylpentanoic acid. GO:0051539Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0003861Catalysis of the reaction: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. +25 total
0.113 Hit 26.8% 2.05e-23
Page 1 of 1 · 9 total proteins