Protein target profile

VK055_0821

hydroxyisourate hydrolase

Genome: KpATCC43816 Gene: uraH AIK79444.1 3D evidence: Experimental + ColabFold model Metabolism 2 reactions UniProt A6T926

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Length 108

Pocket druggability 0.295

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 53 total records

Functional annotation 0 EC 2 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

Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Structure available Experimental + ColabFold model Review the complete evidence below

Risks to review

Microbiome similarity 34 of 4744 screened genomes (0.7%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.29.

Evidence coverage

Core evidence streams are available for this target.

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: 0.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 36.522 Higher values support similarity to known essential genes.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 95.75 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

PDB experimental structure

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 0.295

Structure 3QVA

Pocket Pocket 2

P2Rank

Structure 3QVA

Pocket No pockets

ColabFold model

FPocket 0.495 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 34 / 4744 genomes with a hit

Prevalence 0.7%

Cross-references

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

Metabolic context

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

Explore metabolic network

Metabolic context: no human homolog detected.

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSTLSTHILDISTGTPAEGVTVSLSREGETLANLVTNAQGRIATFSAAPLPAGHYCLTAETGAWFARAGRESVFTRAQIDFVIGEAAEDHFHLPFLIAPGGWSTYRGS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 GO

Gene Ontology (GO)

GO:0006144 The chemical reactions and pathways involving purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
GO:0033971 Catalysis of the reaction: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H+.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

12 records

Show feature table

Start	End	DB	Term	Name
7	22	ProSitePatterns	PS00768	Transthyretin signature 1.
7	22	InterPro	IPR023418	Transthyretin, thyroxine binding site
2	108	NCBIfam	TIGR02962	hydroxyisourate hydrolase
2	108	InterPro	IPR014306	Hydroxyisourate hydrolase
1	108	Gene3D	G3DSA:2.60.40.180	Transthyretin/hydroxyisourate hydrolase domain
1	108	InterPro	IPR036817	Transthyretin/hydroxyisourate hydrolase domain superfamily
2	108	PANTHER	PTHR10395	URICASE AND TRANSTHYRETIN-RELATED
2	108	InterPro	IPR023416	Transthyretin/hydroxyisourate hydrolase domain
4	107	Pfam	PF00576	HIUase/Transthyretin family
4	107	InterPro	IPR023416	Transthyretin/hydroxyisourate hydrolase domain
1	108	SUPERFAMILY	SSF49472	Transthyretin (synonym: prealbumin)
2	108	CDD	cd05822	TLP_HIUase

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.

Download VMD script Full viewer

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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 #2

0.295

Show in viewer

Surrounding area

All structural evidence 1 experimental · 1 predicted

Structural evidence

1 + 1

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
PDB 3QVA	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
ColabFold VK055_0821	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AZA PDB via homolog 153.1 Da · LogP -1.67 · TPSA 107.3 Open detail RCSB PDB

T44 PDB via homolog Detail RCSB PDB

URN PDB via homolog Detail RCSB PDB

ZINC3861723 ZINC proposed compound · Tanimoto 0.750 Detail ZINC

ZINC3875424 ZINC proposed compound · Tanimoto 0.750 Detail ZINC

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
AZA RCSB PDB	2H0F	O32142	153.1 Da LogP -1.67 TPSA 107.3	✓ Ro5	✓ Clean	`c12c([nH]nn1)NC(=O)NC2=O`
T44 RCSB PDB	3Q1E	Q06S87-2	776.9 Da LogP 4.56 TPSA 92.8	1 viol.	✓ Clean	`c1c(cc(c(c1I)Oc2cc(c(c(c2)I)O)I)I)C[C@@H](C(=O)…`
URN RCSB PDB	2H0J	O32142	142.1 Da LogP -1.77 TPSA 117.8	✓ Ro5	✓ Clean	`C1(=C(NC(=O)NC1=O)N)N`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC3861723 ZINC	0.750	433.0 Da LogP 1.56 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1cc(I)c(O)c(I)c1)C(=O)O`
ZINC3875424 ZINC	0.750	433.0 Da LogP 1.56 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1cc(I)c(O)c(I)c1)C(=O)O`
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC1713868 ZINC	0.675	321.1 Da LogP 1.26 TPSA 83.6	✓ Ro5	✓ Clean	`Cc1cc(C[C@H](N)C(=O)O)cc(I)c1O`
ZINC17353379 ZINC	0.675	321.1 Da LogP 1.26 TPSA 83.6	✓ Ro5	✓ Clean	`Cc1cc(C[C@@H](N)C(=O)O)cc(I)c1O`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC13560821 ZINC	0.585	447.0 Da LogP 1.64 TPSA 72.5	✓ Ro5	✓ Clean	`COC(=O)[C@H](N)Cc1cc(I)c(O)c(I)c1`
ZINC15119189 ZINC	0.585	447.0 Da LogP 1.64 TPSA 72.5	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)Cc1cc(I)c(O)c(I)c1`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC4513897 ZINC	0.575	432.0 Da LogP 1.43 TPSA 89.3	✓ Ro5	✓ Clean	`Nc1c(I)cc(C[C@H](N)C(=O)O)cc1I`
ZINC4513900 ZINC	0.575	432.0 Da LogP 1.43 TPSA 89.3	✓ Ro5	✓ Clean	`Nc1c(I)cc(C[C@@H](N)C(=O)O)cc1I`
ZINC4744407 ZINC	0.571	461.0 Da LogP 2.03 TPSA 72.5	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](N)Cc1cc(I)c(O)c(I)c1`
ZINC71782800 ZINC	0.571	461.0 Da LogP 2.03 TPSA 72.5	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H](N)Cc1cc(I)c(O)c(I)c1`
ZINC6239843 ZINC	0.565	253.0 Da LogP -0.75 TPSA 91.7	✓ Ro5	✓ Clean	`Nc1[nH]c(=O)[nH]c(=O)c1I`
ZINC967243 ZINC	0.565	206.0 Da LogP -0.59 TPSA 91.7	✓ Ro5	✓ Clean	`Nc1[nH]c(=O)[nH]c(=O)c1Br`
ZINC146315135 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC1850353 ZINC	0.556	206.1 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC(O)(CC(=O)O)CC(=O)O`
ZINC6092925 ZINC	0.553	399.2 Da LogP 2.74 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)c(I)c2)cc1)C(=O)O`
ZINC57299 ZINC	0.537	339.0 Da LogP 1.87 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1cc(Br)c(O)c(Br)c1)C(=O)O`
ZINC57300 ZINC	0.537	339.0 Da LogP 1.87 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1cc(Br)c(O)c(Br)c1)C(=O)O`
ZINC1575 ZINC	0.535	307.1 Da LogP 0.95 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)c(I)c1)C(=O)O`
ZINC2015200 ZINC	0.535	227.2 Da LogP 0.06 TPSA 113.0	✓ Ro5	✓ Clean	`COc1c(O)cc(C[C@H](N)C(=O)O)cc1O`
ZINC391106 ZINC	0.535	307.1 Da LogP 0.95 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)c(I)c1)C(=O)O`
ZINC2387178 ZINC	0.531	399.2 Da LogP 2.74 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)cc2)c(I)c1)C(=O)O`
ZINC59761244 ZINC	0.525	417.0 Da LogP 1.85 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1cc(I)cc(I)c1)C(=O)O`
ZINC19840845 ZINC	0.524	225.2 Da LogP 0.66 TPSA 81.8	✓ Ro5	✓ Clean	`COc1cc(C[C@@H](N)C(=O)O)cc(OC)c1`
ZINC19840846 ZINC	0.524	225.2 Da LogP 0.66 TPSA 81.8	✓ Ro5	✓ Clean	`COc1cc(C[C@H](N)C(=O)O)cc(OC)c1`
ZINC13398014 ZINC	0.522	220.2 Da LogP -1.07 TPSA 110.1	✓ Ro5	✓ Clean	`COC(=O)CC(O)(CC(=O)OC)C(=O)O`
ZINC3861629 ZINC	0.522	206.1 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C(O)(CC(=O)O)CC(=O)O`
ZINC16922794 ZINC	0.521	431.1 Da LogP 3.66 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@H](Cc1cc(Br)c(Oc2ccc(O)cc2)c(Br)c1)C(=O)O`
ZINC1711133 ZINC	0.521	431.1 Da LogP 3.66 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1cc(Br)c(Oc2ccc(O)cc2)c(Br)c1)C(=O)O`
ZINC4758234 ZINC	0.520	206.2 Da LogP -2.71 TPSA 151.9	✓ Ro5	✓ Clean	`Nc1[nH]c(=O)[nH]c(=O)c1S(N)(=O)=O`
ZINC79036542 ZINC	0.512	211.2 Da LogP -0.49 TPSA 135.6	✓ Ro5	✓ Clean	`Nc1cc(C[C@H](N)C(=O)O)cc(N)c1O`
ZINC32625192 ZINC	0.511	211.2 Da LogP 0.36 TPSA 92.8	✓ Ro5	✓ Clean	`COc1cc(O)cc(C[C@@H](N)C(=O)O)c1`
ZINC32625193 ZINC	0.511	211.2 Da LogP 0.36 TPSA 92.8	✓ Ro5	✓ Clean	`COc1cc(O)cc(C[C@H](N)C(=O)O)c1`
ZINC100969993 ZINC	0.500	359.5 Da LogP 2.70 TPSA 123.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC100969996 ZINC	0.500	359.5 Da LogP 2.70 TPSA 123.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC1746050 ZINC	0.500	250.1 Da LogP 1.65 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1cc(Cl)c(O)c(Cl)c1)C(=O)O`
ZINC19482080 ZINC	0.500	255.3 Da LogP 0.67 TPSA 91.0	✓ Ro5	✓ Clean	`COc1cc(C[C@@H](N)C(=O)O)cc(OC)c1OC`
ZINC19482082 ZINC	0.500	255.3 Da LogP 0.67 TPSA 91.0	✓ Ro5	✓ Clean	`COc1cc(C[C@H](N)C(=O)O)cc(OC)c1OC`
ZINC6091244 ZINC	0.500	217.2 Da LogP 0.62 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1cc(F)c(O)c(F)c1)C(=O)O`
ZINC6091245 ZINC	0.500	217.2 Da LogP 0.62 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1cc(F)c(O)c(F)c1)C(=O)O`
ZINC901726 ZINC	0.500	250.1 Da LogP 1.65 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1cc(Cl)c(O)c(Cl)c1)C(=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.

VK055_0821

Promising target candidate with multiple supporting evidence streams.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Structure

Pathways

Metabolic context

Sequence

Functional annotations

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · FPocket

Structural evidence

Ligand evidence