KpATCC43816 Protein target profile

diaminopimelate decarboxylase

Accession: VK055_4273

Gene: AIK82817.1 lysA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GSP6

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Length 420

Pocket druggability (P2Rank · AlphaFold DB model) 0.912

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 56 total records

Functional annotation 1 EC 4 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

Central metabolic position More central than 96.7% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. 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. 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: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 33.179 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.53 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) 0.912

Structure A0A0H3GSP6

Pocket Pocket 1

Druggability (FPocket) 0.265

Structure A0A0H3GSP6

Pocket Pocket 10

ColabFold model

P2Rank 0.957 · Pocket 1

FPocket 0.501 · Pocket 16

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 111 / 4744 genomes with a hit

Prevalence 2.3%

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 96.7% of genes in this genome, no human homolog detected.

Relative network centrality 96.7% more central than 96.7% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MPHSLYATDTDLTADNLLRLPAEFGCPVWVYDAQIIRRQIAQLSQFDVVRFAQKACSNIHILRLMREQGVKVDSVSLGEIERALAAGYDPQQNPEDIVFTADLIDDATLDRVKALQIPVNAGSIDMLSQLGEVSPGHRVWLRVNPGFGHGHSQKTNTGGENSKHGIWYSHLPAALEVMRRYQLQLVGIHMHIGSGVDYGHLEQVCGAMVRQVVDFGQDLQAISAGGGLSIPYREGEEAIDTAHYYGLWNRAREQIAAHLGHPVKLEIEPGRFLVAESGVLVSQVRSVKEMGSRHFVLIDAGFNDLMRPAMYGSYHHITALAGDGRDLSAAPQVETVVAGPLCESGDVFTQQEGGKVETRLLPAVAPGDYLVLHDTGAYGASMSSNYNSRPLLPEVLFDGGKARLIRRRQTIQELLALELI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

4.1.1.20

Gene Ontology (GO)

GO:0003824 Catalysis 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:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
GO:0008836 Catalysis of the reaction: meso-2,6-diaminopimelate + H+ = L-lysine + CO2.
GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
216	229	ProSitePatterns	PS00879	Orn/DAP/Arg decarboxylases family 2 signature 2.
216	229	InterPro	IPR022657	Orn/DAP/Arg decarboxylase 2, conserved site
276	376	Pfam	PF00278	Pyridoxal-dependent decarboxylase, C-terminal sheet domain
276	376	InterPro	IPR022643	Orn/DAP/Arg decarboxylase 2, C-terminal
25	277	SUPERFAMILY	SSF51419	PLP-binding barrel
25	277	InterPro	IPR029066	PLP-binding barrel
12	416	PANTHER	PTHR43727	DIAMINOPIMELATE DECARBOXYLASE
274	416	FunFam	G3DSA:2.40.37.10:FF:000007	Diaminopimelate decarboxylase
293	311	PRINTS	PR01181	Diaminopimelate decarboxylase signature
293	311	InterPro	IPR002986	Diaminopimelate decarboxylase, LysA
69	86	PRINTS	PR01181	Diaminopimelate decarboxylase signature
69	86	InterPro	IPR002986	Diaminopimelate decarboxylase, LysA
157	166	PRINTS	PR01181	Diaminopimelate decarboxylase signature
157	166	InterPro	IPR002986	Diaminopimelate decarboxylase, LysA
386	408	PRINTS	PR01181	Diaminopimelate decarboxylase signature
386	408	InterPro	IPR002986	Diaminopimelate decarboxylase, LysA
33	279	FunFam	G3DSA:3.20.20.10:FF:000009	Diaminopimelate decarboxylase
376	389	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
376	389	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
51	69	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
51	69	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
71	83	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
71	83	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
265	284	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
265	284	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
182	195	PRINTS	PR01179	Ornithine/diaminopimelate/arginine (ODA) decarboxylase family signature
182	195	InterPro	IPR000183	Ornithine/DAP/Arg decarboxylase
24	397	CDD	cd06828	PLPDE_III_DapDC
24	397	InterPro	IPR002986	Diaminopimelate decarboxylase, LysA
33	279	Gene3D	G3DSA:3.20.20.10	Alanine racemase
33	279	InterPro	IPR029066	PLP-binding barrel
51	69	ProSitePatterns	PS00878	Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site.
51	69	InterPro	IPR022653	Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding site
250	419	SUPERFAMILY	SSF50621	Alanine racemase C-terminal domain-like
250	419	InterPro	IPR009006	Alanine racemase/group IV decarboxylase, C-terminal
14	419	Hamap	MF_02120	Diaminopimelate decarboxylase [lysA].
14	419	InterPro	IPR002986	Diaminopimelate decarboxylase, LysA
8	418	NCBIfam	TIGR01048	diaminopimelate decarboxylase
8	418	InterPro	IPR002986	Diaminopimelate decarboxylase, LysA
22	416	Gene3D	G3DSA:2.40.37.10	Lyase, Ornithine Decarboxylase; Chain A, domain 1
22	416	InterPro	IPR009006	Alanine racemase/group IV decarboxylase, C-terminal
33	275	Pfam	PF02784	Pyridoxal-dependent decarboxylase, pyridoxal binding domain
33	275	InterPro	IPR022644	Orn/DAP/Arg decarboxylase 2, N-terminal

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

0.912

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Surrounding area

Pocket 2 P2Rank #2

0.053

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Surrounding area

Pocket 3 P2Rank #3

0.047

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Surrounding area

Pocket 4 P2Rank #4

0.017

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Surrounding area

Pocket 5 P2Rank #5

0.009

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #10

0.265

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Surrounding area

Residue sets

UniProt: Active site:342-342 Proton donor

UniProt: Binding site:227-227

UniProt: Binding site:268-271

UniProt: Binding site:271-271

UniProt: Binding site:307-307

UniProt: Binding site:311-311

UniProt: Binding site:343-343

UniProt: Binding site:378-378

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.957

Likely same site as FPocket 1 1.3 Å 37 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.048

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Surrounding area

Pocket 3 P2Rank #3

0.044

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Surrounding area

Pocket 4 P2Rank #4

0.03

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #16

0.501

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Surrounding area

Pocket 2 FPocket #1

0.377 Unusual size

Likely same site as P2Rank 1 1.3 Å 37 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:342-342 Proton donor

UniProt: Binding site:227-227

UniProt: Binding site:268-271

UniProt: Binding site:271-271

UniProt: Binding site:307-307

UniProt: Binding site:311-311

UniProt: Binding site:343-343

UniProt: Binding site:378-378

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_A0A0H3GSP6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4273	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

AZ1 PDB via homolog 188.2 Da · LogP 1.89 · TPSA 74.6 Open detail RCSB PDB

DN9 PDB via homolog Detail RCSB PDB

LLP PDB via homolog Detail RCSB PDB

N2P PDB via homolog Detail RCSB PDB

TME PDB via homolog Detail RCSB PDB

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
AZ1 RCSB PDB	1TUF	Q58497	188.2 Da LogP 1.89 TPSA 74.6	✓ Ro5	✓ Clean	`C(CCCC(=O)O)CCCC(=O)O`
DN9 RCSB PDB	6KNK	A0A0H3JPF2	465.4 Da LogP -1.41 TPSA 235.8	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNCCNC(=O)C[C@](CC(=O)…`
LLP RCSB PDB	4XG1	A1SR00	375.3 Da LogP 0.71 TPSA 175.6	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/CCCCC(C(=O)O)N)O`
N2P RCSB PDB	5GJP	O50657	102.2 Da LogP 0.07 TPSA 52.0	✓ Ro5	✓ Clean	`C(CCN)CCN`
TME RCSB PDB	4XG1	A1SR00	44.1 Da LogP 1.42 TPSA 0.0	✓ Ro5	✓ Clean	`CCC`
X3J RCSB PDB	6KNK	A0A0H3JPF2	234.2 Da LogP -2.26 TPSA 150.0	✓ Ro5	✓ Clean	`C(CNC(=O)C[C@](CC(=O)O)(C(=O)O)O)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
ZINC1529497 ZINC	1.000	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	1.000	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115 ZINC	1.000	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1685531 ZINC	1.000	200.4 Da LogP 2.80 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCN`
ZINC1700020 ZINC	1.000	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC34273707 ZINC	1.000	256.5 Da LogP 4.37 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCCN`
ZINC3860440 ZINC	1.000	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298 ZINC	1.000	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062 ZINC	1.000	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC5178646 ZINC	1.000	228.4 Da LogP 3.59 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCN`
ZINC26897400 ZINC	0.800	286.4 Da LogP 3.41 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCCC(=O)O`
ZINC3074813 ZINC	0.800	258.3 Da LogP 2.63 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCCCC(=O)O`
ZINC34423725 ZINC	0.800	342.5 Da LogP 4.97 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC4822898 ZINC	0.800	272.3 Da LogP 3.02 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCC(=O)O`
ZINC4822900 ZINC	0.800	300.4 Da LogP 3.80 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O`
ZINC14686440 ZINC	0.759	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	0.759	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	0.759	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(=…`
ZINC13433578 ZINC	0.750	201.3 Da LogP 1.68 TPSA 80.4	✓ Ro5	✓ Clean	`NC(=O)CCCCCCCCC(=O)O`
ZINC14510370 ZINC	0.750	244.4 Da LogP 3.74 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCO`
ZINC1531061 ZINC	0.750	216.3 Da LogP 2.96 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCO`
ZINC1610426 ZINC	0.750	230.3 Da LogP 3.35 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCO`
ZINC2168567 ZINC	0.750	202.3 Da LogP 2.57 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCO`
ZINC3074815 ZINC	0.750	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCC(=O)O`
ZINC3861297 ZINC	0.750	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCO`
ZINC4284502 ZINC	0.750	258.4 Da LogP 4.13 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCO`
ZINC5287109 ZINC	0.750	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCCO`
ZINC2508031 ZINC	0.733	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)CCCCC(=O)O`
ZINC2114966 ZINC	0.724	332.2 Da LogP 0.99 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(/C=N/CCCC(=O)O)c1O`
ZINC12954423 ZINC	0.706	232.4 Da LogP 3.90 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCS`
ZINC13357569 ZINC	0.706	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCC(=O)O`
ZINC138216182 ZINC	0.706	293.2 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCBr`
ZINC14619253 ZINC	0.706	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCC(=O)O`
ZINC1529498 ZINC	0.706	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
ZINC1530417 ZINC	0.706	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
ZINC1628119 ZINC	0.706	214.3 Da LogP 4.38 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)O`
ZINC1763117 ZINC	0.706	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCC(=O)O`
ZINC1841307 ZINC	0.706	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCCC(=O)O`
ZINC1845814 ZINC	0.706	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCC(=O)O`
ZINC1845839 ZINC	0.706	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCC(=O)O`
ZINC2164257 ZINC	0.706	218.4 Da LogP 3.51 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCS`
ZINC22048354 ZINC	0.706	229.4 Da LogP 3.32 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCC(=O)O`
ZINC33822328 ZINC	0.706	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCCCCCC(=O)O`
ZINC34552398 ZINC	0.706	257.4 Da LogP 4.10 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCC(=O)O`
ZINC34628306 ZINC	0.706	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCC(=O)O`
ZINC35465466 ZINC	0.706	244.3 Da LogP 2.24 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCC(=O)CCC(=O)O`
ZINC5855130 ZINC	0.706	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCCCC(=O)O`
ZINC90745150 ZINC	0.706	260.4 Da LogP 4.68 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCS`
ZINC4789573 ZINC	0.667	310.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCC#CCCCCCCCC(=O)O`
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`

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.

Sequence

UniProt A0A0H3GSP6

Pathways

KEGG R00451 BioCyc DIAMINOPIMDECARB-RXN