KpATCC43816 Protein target profile

deoC/LacD aldolase family protein

Accession: VK055_3965

Gene: AIK82513.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3H3A9
Length 295
Pocket druggability (P2Rank · AlphaFold DB model) 0.858
Direct ligand evidence 0 56 total records
Functional annotation 0 EC 3 GO
Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target
No hit
Gut microbiome similarity
4.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
N
DEG identity (%)
0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT
95.56 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.858
Structure A0A0H3H3A9
Pocket Pocket 1
Druggability (FPocket) 0.116
Structure A0A0H3H3A9
Pocket Pocket 3
ColabFold model
P2Rank 0.876 · Pocket 1
FPocket 0.355 · Pocket 2
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 225 / 4744 genomes with a hit
Prevalence 4.7%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MADLDDIKEGKDFGIDRPQQNTLYTLKGCGSLDWGMQSRLARIFNPHSNRTVMLAFDHGYFQGPTTGLERIDLSIAPLFADTDVLMCTRGVLRSQVPAATNKPVVLRASGGNSILSELSNECVAVAMEDALRLNVCAVAAQVYIGSEYEHQSINNIIKLVDAGNRYGMPVLAVTGVGKEMTRDARYFSLASRIAAEMGAQFVKTYFVEEGFEKVTASCPVPIVIAGGKKLPEHEALEMCWRAIDQGASGVDMGRNIFQSSAPRAMLKAVKKVVHENLNAREAYQFWQEEKQGELK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Subcellular localization

Localization
Cytoplasmic

Gene Ontology (GO)

3
  • GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
  • GO:0016829 Catalysis 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:0004332 Catalysis of the reaction: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

13 records
Show feature table
Start End DB Term Name
32 287 PANTHER PTHR47916 FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1
51 259 Pfam PF01791 DeoC/LacD family aldolase
51 259 InterPro IPR002915 DeoC/FbaB/LacD aldolase
35 275 SUPERFAMILY SSF51569 Aldolase
1 291 Gene3D G3DSA:3.20.20.70 Aldolase class I
1 291 InterPro IPR013785 Aldolase-type TIM barrel
31 289 PIRSF PIRSF038992 Aldolase_Ia
31 289 InterPro IPR041720 Aldolase FbaB-like, archaeal-type
1 291 Hamap MF_02052 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase [lsrF].
1 291 InterPro IPR033673 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
51 274 CDD cd00958 DhnA
51 274 InterPro IPR041720 Aldolase FbaB-like, archaeal-type
51 259 SMART SM01133 DeoC_2

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low
How colors and pocket overlays are used
Uniform protein color marks the displayed model as a single molecular object.
Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.
Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.
'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.
'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.
'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.
Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1
0.858
Show in viewer
Surrounding area
Pocket 2 P2Rank #2
0.026
Show in viewer
Surrounding area
Pocket 3 P2Rank #3
0.014
Show in viewer
Surrounding area
Pocket 4 P2Rank #4
0.009
Show in viewer
Surrounding area
Residue sets
UniProt: Active site:203-203 Schiff-base intermediate with substrate
All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold DB AF_A0A0H3H3A9
AlphaFold DB full sequence Viewing
ColabFold VK055_3965
ColabFold full sequence Loaded

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

56 records
Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records
Transferred evidence 6 records from similar proteins
Structural ligands 6 0 loaded crystals
Measured bioactivity 0 direct and transferred ChEMBL records
Proposed compounds 50 similarity-based ZINC candidates
Best available ligand signal
13P PDB via homolog 170.1 Da · LogP -1.34 · TPSA 104.1 Open detail RCSB PDB
26T PDB via homolog Detail RCSB PDB
5RP PDB via homolog Detail RCSB PDB
F2P PDB via homolog Detail RCSB PDB
M2P PDB via homolog Detail RCSB PDB

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
13P RCSB PDB Q57843 170.1 Da LogP -1.34 TPSA 104.1 ✓ Ro5 ✓ Clean C(C(=O)COP(=O)(O)O)O
26T RCSB PDB P76143 212.1 Da LogP -1.39 TPSA 121.1 ✓ Ro5 ✓ Clean CC(=O)[C@H](C(=O)COP(=O)(O)O)O
5RP RCSB PDB P76143 230.1 Da LogP -2.62 TPSA 144.5 ✓ Ro5 ✓ Clean C([C@H]([C@H](C(=O)CO)O)O)OP(=O)(O)O
F2P RCSB PDB Q57843 342.1 Da LogP -3.35 TPSA 214.4 1 viol. ✓ Clean C([C@H]([C@H]([C@H]([C@H](COP(=O)(O)O)O)O)O)O)O…
M2P RCSB PDB P58315 342.1 Da LogP -3.35 TPSA 214.4 1 viol. ✓ Clean C([C@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)O…
R5P RCSB PDB P76143 230.1 Da LogP -2.62 TPSA 144.5 ✓ Ro5 ✓ Clean C(C(C(C(C=O)O)O)O)OP(=O)(O)O

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.