Protein target profile

VK055_0608

muconate cycloisomerase

Genome: KpATCC43816 Gene: AIK79231.1 catB 3D evidence: Experimental + ColabFold model Metabolism 1 reaction UniProt A6T9N5

Export view

Length 372

Pocket druggability 0.804

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 54 total records

Functional annotation 0 EC 4 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Central metabolic position More central than 94.5% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Review the complete evidence below

Risks to review

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 (%): 29.477 Higher values support similarity to known essential genes.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 97.3 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 0.804

Structure 3FCP

Pocket Pocket 2

P2Rank 0.722

Structure 3FCP

Pocket Pocket 1

ColabFold model

FPocket 0.349 · Pocket 16

P2Rank 0.409 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 35 / 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

Attractive metabolic target: catalyzes a producing & consuming chokepoint reaction, no isoenzyme backup detected, more central than 94.5% of genes in this genome, no human homolog detected.

Relative network centrality 94.5% more central than 94.5% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTATVEQIESWIVDVPTIRPHKLSMTTMGCQSLVIVRLTRSDGICGIGEATTIGGLSYGVESPEAISSAITHYLTPLLKGQPADNLNALTARMNGAIKGNTFAKSAIETALLDAQGKALGLPVSALLGGALQTALPVLWTLASGDTAKDIAEGEKLLAEGRHRAFKLKIGARELATDLRHTRAIVEALGDRASIRVDVNQAWDAATGAKGCRELAAMGVDLIEQPVSAHDNAALVRLSQQIETAILADEAVATAYDGYQLAQQGFTGAYALKIAKAGGPNSVLALARVAQAAGIGLYGGTMLEGTVGTVASLHAWSTLPLQWGTEMFGPLLLKDDIVSVPLTFADGQVALPQTPGLGVELDEDKLHFYTRQP

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

GO:0030145 Binding to a manganese ion (Mn).
GO:0009063 The chemical reactions and pathways resulting in the breakdown of amino acids, organic acids containing one or more amino substituents.
GO:0018849 Catalysis of the reaction: 2,5-dihydro-5-oxofuran-2-acetate = cis,cis-hexadienedioate.
GO:0018850 Catalysis of the reaction: 2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
4	129	SUPERFAMILY	SSF54826	Enolase N-terminal domain-like
4	129	InterPro	IPR029017	Enolase-like, N-terminal
6	371	NCBIfam	TIGR02534	muconate/chloromuconate family cycloisomerase
6	371	InterPro	IPR013370	Muconate/chloromuconate cycloisomerase
2	371	SFLD	SFLDG01258	(chloro)muconate cycloisomerase (syn) like
2	371	InterPro	IPR013370	Muconate/chloromuconate cycloisomerase
121	355	Gene3D	G3DSA:3.20.20.120	-
121	355	InterPro	IPR036849	Enolase-like, C-terminal domain superfamily
33	365	Gene3D	G3DSA:3.30.390.10	-
33	365	InterPro	IPR029017	Enolase-like, N-terminal
154	363	Pfam	PF13378	Enolase C-terminal domain-like
154	363	InterPro	IPR029065	Enolase C-terminal domain-like
147	244	SMART	SM00922	MR_MLE_2
147	244	InterPro	IPR013342	Mandelate racemase/muconate lactonizing enzyme, C-terminal
2	371	SFLD	SFLDG00180	muconate cycloisomerase
116	371	SUPERFAMILY	SSF51604	Enolase C-terminal domain-like
116	371	InterPro	IPR036849	Enolase-like, C-terminal domain superfamily
9	128	Pfam	PF02746	Mandelate racemase / muconate lactonizing enzyme, N-terminal domain
9	128	InterPro	IPR013341	Mandelate racemase/muconate lactonizing enzyme, N-terminal domain
2	366	PANTHER	PTHR48073	O-SUCCINYLBENZOATE SYNTHASE-RELATED
103	128	ProSitePatterns	PS00908	Mandelate racemase / muconate lactonizing enzyme family signature 1.
103	128	InterPro	IPR018110	Mandelate racemase/muconate lactonizing enzyme, conserved site
4	365	CDD	cd03318	MLE
4	365	InterPro	IPR013370	Muconate/chloromuconate cycloisomerase

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

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.804

Likely same site as P2Rank 1 6.5 Å 17 shared residues 81% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #19

0.236

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.722

Likely same site as FPocket 2 6.5 Å 17 shared residues 81% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.19

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.118

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.005

Likely same site as FPocket 2 6.7 Å 6 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.002

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.409

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.106

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.019

Likely same site as FPocket 18 1.8 Å 9 shared residues 100% of smaller site

Show in viewer

Surrounding area

Site 4 P2Rank #4

0.019

Show in viewer

Surrounding area

Site 5 P2Rank #5

0.009

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:189-189 Proton acceptor

UniProt: Active site:346-346 Proton donor

UniProt: Binding site:220-220

UniProt: Binding site:269-269

UniProt: Binding site:270-270

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 3FCP	X-ray	—	A	—	PDBe RCSB PDBj File	Viewing
ColabFold VK055_0608	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

MUC PDB via homolog 142.1 Da · LogP -0.06 · TPSA 63.6 Open detail RCSB PDB

NLQ PDB via homolog Detail RCSB PDB

NSK PDB via homolog Detail RCSB PDB

SUG PDB via homolog Detail RCSB PDB

ZINC2558958 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
MUC RCSB PDB	3DG6	A0QTN8	142.1 Da LogP -0.06 TPSA 63.6	✓ Ro5	✓ Clean	`C1=CC(=O)O[C@H]1CC(=O)O`
NLQ RCSB PDB	1XPY	Q9RYA6	188.2 Da LogP -1.16 TPSA 109.5	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCC(=O)N)C(=O)O`
NSK RCSB PDB	2P8B	Q81IL5	246.3 Da LogP -0.45 TPSA 129.7	✓ Ro5	✓ Clean	`C(CCN)C[C@@H](C(=O)O)NC(=O)CCC(=O)O`
SUG RCSB PDB	2P8C	Q81IL5	274.3 Da LogP -1.32 TPSA 165.6	1 viol.	✓ Clean	`C(C[C@@H](C(=O)O)NC(=O)CCC(=O)O)CNC(=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
ZINC2558958 ZINC	0.750	259.3 Da LogP -1.65 TPSA 138.6	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC37452968 ZINC	0.706	287.3 Da LogP -1.02 TPSA 138.6	✓ Ro5	✓ Clean	`CC(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)O)C(C)C`
ZINC37452969 ZINC	0.706	287.3 Da LogP -1.02 TPSA 138.6	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](C(=O)N[C@@H](CCC(N)=O)C(=O)O)C(C)C`
ZINC2558960 ZINC	0.697	245.2 Da LogP -2.04 TPSA 138.6	✓ Ro5	✓ Clean	`CC(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC2504612 ZINC	0.656	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC2560934 ZINC	0.656	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC2560982 ZINC	0.656	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC4523272 ZINC	0.656	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC5167289 ZINC	0.656	315.3 Da LogP -3.01 TPSA 187.5	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(…`
ZINC2555108 ZINC	0.645	203.2 Da LogP -2.22 TPSA 135.5	✓ Ro5	✓ Clean	`NCC(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC2561012 ZINC	0.645	203.2 Da LogP -2.22 TPSA 135.5	✓ Ro5	✓ Clean	`NCC(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC1664046 ZINC	0.625	206.2 Da LogP -1.21 TPSA 109.5	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CF)C(=O)O`
ZINC2048484 ZINC	0.625	206.2 Da LogP -1.21 TPSA 109.5	✓ Ro5	✓ Clean	`NC(=O)CC[C@@H](NC(=O)CF)C(=O)O`
ZINC2391099 ZINC	0.625	274.3 Da LogP -2.59 TPSA 178.6	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC2522563 ZINC	0.618	245.3 Da LogP -1.20 TPSA 135.5	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC54075863 ZINC	0.618	231.3 Da LogP -1.57 TPSA 121.5	✓ Ro5	✓ Clean	`CN[C@@H](C)C(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC1532510 ZINC	0.606	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=…`
ZINC1532511 ZINC	0.606	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O…`
ZINC1532512 ZINC	0.606	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC1532513 ZINC	0.606	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC1618887 ZINC	0.606	242.2 Da LogP -0.62 TPSA 109.5	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)C(F)(F)F)C(=O)O`
ZINC2383349868 ZINC	0.605	486.6 Da LogP 1.83 TPSA 206.0	1 viol.	✓ Clean	`N=C(NCCC[C@H](NC(=O)CCCCCCC(=O)O)C(=O)O)NC(=O)C…`
ZINC1576318 ZINC	0.600	246.3 Da LogP 0.23 TPSA 118.7	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC2390893 ZINC	0.600	246.3 Da LogP 0.23 TPSA 118.7	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC2522621 ZINC	0.600	247.3 Da LogP -2.47 TPSA 155.7	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC12494450 ZINC	0.588	217.2 Da LogP -0.98 TPSA 121.5	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCCNC(N)=O)C(=O)O`
ZINC2390999 ZINC	0.588	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC2504638 ZINC	0.588	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=…`
ZINC2522620 ZINC	0.588	261.2 Da LogP -2.38 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)[C@@H](N)CC(=O)O)C(=O)O`
ZINC4534089 ZINC	0.588	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=O…`
ZINC4534090 ZINC	0.588	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O…`
ZINC4534091 ZINC	0.588	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)N[C@H](CCC(=O)O)C(=O)O)C(=O)O`
ZINC100652190 ZINC	0.583	300.4 Da LogP 1.96 TPSA 109.5	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC100654638 ZINC	0.583	328.5 Da LogP 2.74 TPSA 109.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC1786138 ZINC	0.583	259.3 Da LogP -0.81 TPSA 135.5	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC1786139 ZINC	0.583	259.3 Da LogP -0.81 TPSA 135.5	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC1786141 ZINC	0.583	259.3 Da LogP -0.81 TPSA 135.5	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC1786143 ZINC	0.583	259.3 Da LogP -0.81 TPSA 135.5	✓ Ro5	✓ Clean	`CC(C)C[C@@H](N)C(=O)N[C@H](CCC(N)=O)C(=O)O`
ZINC2567650 ZINC	0.583	288.3 Da LogP -2.33 TPSA 164.6	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C…`
ZINC28539029 ZINC	0.583	328.5 Da LogP 2.74 TPSA 109.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC77286434 ZINC	0.583	300.4 Da LogP 1.96 TPSA 109.5	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC4545855 ZINC	0.574	403.4 Da LogP -4.15 TPSA 249.8	1 viol.	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)CN)C(=O)NCC(=O)N[C@@H](CC…`
ZINC1847640 ZINC	0.571	216.2 Da LogP -1.16 TPSA 128.3	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCCNC(=N)N)C(=O)O`
ZINC1857793110 ZINC	0.571	230.3 Da LogP -0.12 TPSA 95.5	✓ Ro5	✓ Clean	`CCCNC(=O)CC[C@@H](NC(C)=O)C(=O)O`
ZINC1857793111 ZINC	0.571	230.3 Da LogP -0.12 TPSA 95.5	✓ Ro5	✓ Clean	`CCCNC(=O)CC[C@H](NC(C)=O)C(=O)O`
ZINC2169795 ZINC	0.571	216.2 Da LogP -1.16 TPSA 128.3	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CCCNC(=N)N)C(=O)O`
ZINC2560343 ZINC	0.571	245.3 Da LogP 0.70 TPSA 92.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCC(=O)OC(C)(C)C)C(=O)O`
ZINC2560992 ZINC	0.571	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC65356644 ZINC	0.571	245.3 Da LogP 0.70 TPSA 92.7	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CCC(=O)OC(C)(C)C)C(=O)O`
ZINC1677520 ZINC	0.568	278.3 Da LogP 0.13 TPSA 128.3	✓ Ro5	✓ Clean	`N=C(N)NCCC[C@H](NC(=O)c1ccccc1)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_0608

Strong target candidate with converging metabolic, structural and chemical evidence.

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 · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence