Protein target profile

KP13_04095

Aldehyde dehydrogenase

Genome: KpKP13 Gene: AHE43096.1 aldA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A060VEA6
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Length 506
Pocket druggability 0.96
Direct ligand evidence 0 162 total records
Functional annotation 2 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.

Main supporting evidence

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.96, P2Rank 0.92). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.96. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.92. Review the complete evidence below

Risks to review

Human similarity Top human hit identity: 45.333%. This target also has a predicted binding pocket (FPocket 0.96) — check the ligand evidence before deprioritizing on off-target risk alone. Microbiome similarity 189 of 4744 screened genomes (4.0%) have a significant similarity hit. This target also has a predicted binding pocket (FPocket 0.96) — check the ligand evidence before deprioritizing on off-target risk alone.

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for 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
Hit
Human identity (%)
45.333 Lower values reduce human off-target concern.
Human E-value
1.2199999999999999e-54
Gut microbiome similarity
4.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
Y
DEG identity (%)
40.625 Higher values support similarity to known essential genes.
DEG E-value
4.24e-121 Smaller values mean stronger essential-gene similarity.

Localization

Localization
Cytoplasmic

Structure confidence

ColabFold pLDDT
97.96 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.96
Structure A0A060VEA6
Pocket Pocket 1
P2Rank 0.917
Structure A0A060VEA6
Pocket Pocket 1
ColabFold model
FPocket 0.574 · Pocket 8
P2Rank 0.896 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 189 / 4744 genomes with a hit
Prevalence 4.0%

Cross-references

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

Sequence

UniProt A0A060VEA6

Chemistry

ChEMBL CHEMBL3660752 ChEMBL CHEMBL113123 ChEMBL CHEMBL112696 ChEMBL CHEMBL3660748 ChEMBL CHEMBL3660728 ChEMBL CHEMBL3660742 ChEMBL CHEMBL3660747 ChEMBL CHEMBL3660751 ChEMBL CHEMBL3660739 ChEMBL CHEMBL3660744 ChEMBL CHEMBL3660749 ChEMBL CHEMBL3660730 ChEMBL CHEMBL3660732 ChEMBL DWT ChEMBL CHEMBL3660738 ChEMBL CHEMBL112007 ChEMBL CHEMBL113640 ChEMBL CHEMBL3660726 ChEMBL CHEMBL3660727 ChEMBL CHEMBL3660735 ChEMBL DXH ChEMBL CHEMBL3660731 ChEMBL CHEMBL3660741 ChEMBL CHEMBL3660745 ChEMBL CHEMBL3660743 ChEMBL CHEMBL3660722 ChEMBL CHEMBL3667538 ChEMBL CHEMBL3667541 ChEMBL CHEMBL3667547 ChEMBL CHEMBL5723324 ChEMBL CHEMBL4876602 ChEMBL CHEMBL3660746 ChEMBL CHEMBL114083 ChEMBL CHEMBL114397 ChEMBL CHEMBL115092 ChEMBL CHEMBL486422 ChEMBL CHEMBL3660736 ChEMBL CHEMBL3660716 ChEMBL CHEMBL3128207 ChEMBL CHEMBL4861872 ChEMBL CHEMBL3660712 ChEMBL CHEMBL3660721 ChEMBL CHEMBL4859904 ChEMBL CHEMBL3667535 ChEMBL CHEMBL3660740 ChEMBL CHEMBL4286209 ChEMBL CHEMBL113113 ChEMBL CHEMBL4848258 ChEMBL CHEMBL115109 ChEMBL CHEMBL1562069 ChEMBL CHEMBL3660725 ChEMBL CHEMBL3660719 ChEMBL CHEMBL4213331 ChEMBL CHEMBL4875157 ChEMBL CHEMBL4848831 ChEMBL CHEMBL3660723 ChEMBL CHEMBL3660733 ChEMBL CHEMBL4090473 ChEMBL CHEMBL4855442 ChEMBL CHEMBL109641 ChEMBL CHEMBL113586 ChEMBL CHEMBL132065 ChEMBL CHEMBL3128203 ChEMBL CHEMBL4849624 ChEMBL CHEMBL5269320 ChEMBL CHEMBL5283146 ChEMBL CHEMBL3667536 ChEMBL CHEMBL3915386 ChEMBL CHEMBL4847114 ChEMBL CHEMBL4874309 ChEMBL A5Y ChEMBL CHEMBL113058 ChEMBL CHEMBL4642789 ChEMBL CHEMBL4876076 ChEMBL CHEMBL262662 ChEMBL CHEMBL326803 ChEMBL CHEMBL4214509 ChEMBL CHEMBL4217452 ChEMBL CHEMBL4862833 ChEMBL CHEMBL4863668 ChEMBL CHEMBL4873315 ChEMBL CHEMBL109649 ChEMBL CHEMBL111984 ChEMBL CHEMBL4078971 ChEMBL CHEMBL4081886 ChEMBL CHEMBL4873090 ChEMBL CHEMBL3660724 ChEMBL CHEMBL1349972 ChEMBL CHEMBL3667539 ChEMBL CHEMBL3667548 ChEMBL CHEMBL4205216 ChEMBL CHEMBL4216790 ChEMBL CHEMBL3660729 ChEMBL CHEMBL4846491 ChEMBL CHEMBL112165 ChEMBL CHEMBL4213859 ChEMBL CHEMBL4852411 ChEMBL CHEMBL3667537 ChEMBL CHEMBL4867380 ChEMBL CW2

Sequence

Primary amino-acid sequence viewer.

MRYAHPGQPGAVVSFKSAYGNFIDGRFVEPLSGEFFMNTSPVDGSNIAQFPRSDARDIDFALDAAHRAAPAWGKTSVQQRSRLLLQVADRIEQHLEYLAVAESWDNGKPIRETLNADLPLAVDHFRYFAGCLRAQEGSTAEIDETTVAYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPLSITLLLELIGDLFPAGVLNVVQGFGKEAGEALATSKRIAKLAFTGSTPVGRHILACAAENIIPCTVELGGKSPNIYFADVMDGEEEFIEKAVEGLVLGFFNQGEVCTCPSRALIHESIYEPFMARVMEKVAQIRRGDPLDTDTMIGAQASRQQFDKILSYIQIAREEGGQILTGGERAAIAPALDNGFYIQPTLIKGRNDMRSFQEEIFGPVIGVTTFKDEAEALAIANETQFGLGAGVWTRDTNLAYRMGRGIKAGRVWTNCYHVYPAHAAFGGYKQSGVGRETHKMALDAYQQTKNLLVSYGTAPLGLF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 3 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

3
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
  • GO:0050061 Catalysis of the reaction: a long-chain fatty aldehyde + H2O + NAD+ = a long-chain fatty acid + 2 H+ + NADH.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

16 records
Show feature table
Start End DB Term Name
19 498 CDD cd07559 ALDH_ACDHII_AcoD-like
11 503 PANTHER PTHR43111 ALDEHYDE DEHYDROGENASE B-RELATED
265 463 FunFam G3DSA:3.40.309.10:FF:000012 Betaine aldehyde dehydrogenase
261 268 ProSitePatterns PS00687 Aldehyde dehydrogenases glutamic acid active site.
261 268 InterPro IPR029510 Aldehyde dehydrogenase, glutamic acid active site
34 493 Pfam PF00171 Aldehyde dehydrogenase family
34 493 InterPro IPR015590 Aldehyde dehydrogenase domain
14 498 SUPERFAMILY SSF53720 ALDH-like
14 498 InterPro IPR016161 Aldehyde/histidinol dehydrogenase
265 467 Gene3D G3DSA:3.40.309.10 Aldehyde Dehydrogenase; Chain A, domain 2
265 467 InterPro IPR016163 Aldehyde dehydrogenase, C-terminal
294 305 ProSitePatterns PS00070 Aldehyde dehydrogenases cysteine active site.
294 305 InterPro IPR016160 Aldehyde dehydrogenase, cysteine active site
25 492 Gene3D G3DSA:3.40.605.10 Aldehyde Dehydrogenase; Chain A, domain 1
25 492 InterPro IPR016162 Aldehyde dehydrogenase, N-terminal
31 286 FunFam G3DSA:3.40.605.10:FF:000001 Aldehyde dehydrogenase 1

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 · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1
0.96
Likely same site as P2Rank 2 5.1 Å 13 shared residues 100% of smaller site
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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1
0.917
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Surrounding area
Site 2 P2Rank #2
0.487
Likely same site as FPocket 1 5.1 Å 13 shared residues 100% of smaller site
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Surrounding area
Site 3 P2Rank #3
0.1
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Surrounding area
Site 4 P2Rank #4
0.035
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Surrounding area
Site 5 P2Rank #5
0.014
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Surrounding area
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_A0A060VEA6
AlphaFold DB — — full sequence — Viewing
ColabFold KP13_04095
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.

162 records
Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records
Transferred evidence 112 records from similar proteins
Structural ligands 12 0 loaded crystals
Measured bioactivity 100 direct and transferred ChEMBL records
Proposed compounds 50 similarity-based ZINC candidates
Best available ligand signal
2NO PDB via homolog 46.0 Da · LogP 0.10 · TPSA 49.3 Open detail RCSB PDB
3AK PDB via homolog Detail RCSB PDB
BTB PDB via homolog Detail RCSB PDB
BXB PDB via homolog Detail RCSB PDB
CQY 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
2NO RCSB PDB
4FQF
P05091 46.0 Da LogP 0.10 TPSA 49.3 ✓ Ro5 ✓ Clean N(=O)[O]
3AK RCSB PDB
4KWF
P05091 237.3 Da LogP 2.42 TPSA 37.4 ✓ Ro5 ✓ Clean c1ccc(cc1)CN2c3ccccc3C(=O)C2=O
BTB RCSB PDB
4FR8
P05091 209.2 Da LogP -3.01 TPSA 104.4 ✓ Ro5 ✓ Clean C(CO)N(CCO)C(CO)(CO)CO
BXB RCSB PDB
3INJ
P05091 324.2 Da LogP 3.65 TPSA 47.6 ✓ Ro5 ✓ Clean c1cc(c(c(c1)Cl)C(=O)NCc2ccc3c(c2)OCO3)Cl
CQY RCSB PDB
6B5G
O94788 430.5 Da LogP 3.62 TPSA 79.2 ✓ Ro5 ✓ Clean CCOc1ccsc1C(=O)N2CCN(CC2)c3ccc(c(c3)N4CCCC4)[N+…
CRD RCSB PDB
1O01
P05091 70.1 Da LogP 0.76 TPSA 17.1 ✓ Ro5 ✓ Clean C\C=C\C=O
CU4 RCSB PDB
6B5H
O94788 460.5 Da LogP 4.21 TPSA 104.8 ✓ Ro5 ✓ Clean CS(=O)(=O)c1ccc(cc1)c2c(cn(n2)c3ccc(cc3)C#N)C(=…
I3E RCSB PDB
3SZ9
P05091 162.2 Da LogP 2.84 TPSA 17.1 ✓ Ro5 ✓ Clean CCc1ccc(cc1)C(=O)CC
N98 RCSB PDB
6TGW
P47895 373.4 Da LogP 3.58 TPSA 75.0 ✓ Ro5 ✓ Clean COC(=O)c1cc(nc2n1nc(c2)c3ccccc3)c4ccc5c(c4)OCO5
NW8 RCSB PDB
6TRY
P47895 304.8 Da LogP 5.32 TPSA 17.3 1 viol. ✓ Clean c1ccc(cc1)c2cn3cccc(c3n2)c4ccc(cc4)Cl
REA RCSB PDB
5FHZ
P47895 300.4 Da LogP 5.60 TPSA 37.3 1 viol. ✓ Clean CC1=C(C(CCC1)(C)C)/C=C/C(=C/C=C/C(=C/C(=O)O)/C)…
TNG RCSB PDB
4FR8
P05091 227.1 Da LogP -1.02 TPSA 157.1 ✓ Ro5 ✓ Clean C(C(CO[N+](=O)[O-])O[N+](=O)[O-])O[N+](=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.