KpATCC43816 Protein target profile

erythrose-4-phosphate dehydrogenase

Accession: VK055_4126

Gene: AIK82672.1 epd 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GSZ3

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Length 342

Pocket druggability (P2Rank · AlphaFold DB model) 0.685

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 60 total records

Functional annotation 1 EC 6 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 chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.69, FPocket 0.70). Use the 3D pocket comparison to verify whether they identify the same site. Central metabolic position More central than 91.5% 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: Hit
Human identity (%): 38.983 Lower values reduce human off-target concern.
Human E-value: 1.8e-32
Gut microbiome similarity: 3.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 53.03 Higher values support similarity to known essential genes.
DEG E-value: 7.55e-127 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 96.59 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) 0.685

Structure A0A0H3GSZ3

Pocket Pocket 1

Druggability (FPocket) 0.7

Structure A0A0H3GSZ3

Pocket Pocket 8

ColabFold model

P2Rank 0.769 · Pocket 1

FPocket 0.462 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 186 / 4744 genomes with a hit

Prevalence 3.9%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Vitamin B6 metabolism, no isoenzyme backup detected, more central than 91.5% of genes in this genome.

Relative network centrality 91.5% more central than 91.5% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTIRIAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHEPTIAALPWRELAVDVVLDCTGVYGSREHGEAHLQAGAKKVLFSHPGGNDLDATVVYGVNQDELRAGHRIVSNASCTTNCIIPIIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAIAVRVPTINVTAIDLSVTVKKPVKACEVNQLLQKAAQGAFHGIVDYTELPLVSTDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGFANRMLDTTLAMAAIGFRFDA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.2.1.72

Gene Ontology (GO)

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:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0042823 The chemical reactions and pathways resulting in the formation of pyridoxal phosphate, pyridoxal phosphorylated at the hydroxymethyl group of C-5, the active form of vitamin B6.
GO:0048001 Catalysis of the reaction: D-erythrose 4-phosphate + H2O + NAD+ = 4-phospho-D-erythronate + 2 H+ + NADH.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0008615 The chemical reactions and pathways resulting in the formation of pyridoxine, 2-methyl-3-hydroxy-4,5-bis(hydroxymethyl)pyridine, one of the vitamin B6 compounds.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
3	155	SMART	SM00846	gp_dh_n_7
3	155	InterPro	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
160	316	Pfam	PF02800	Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
160	316	InterPro	IPR020829	Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain
3	104	Pfam	PF00044	Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
3	104	InterPro	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
153	160	ProSitePatterns	PS00071	Glyceraldehyde 3-phosphate dehydrogenase active site.
153	160	InterPro	IPR020830	Glyceraldehyde 3-phosphate dehydrogenase, active site
1	337	PIRSF	PIRSF000149	GAPDH
1	337	InterPro	IPR020831	Glyceraldehyde/Erythrose phosphate dehydrogenase family
3	328	Gene3D	G3DSA:3.40.50.720	-
154	318	Gene3D	G3DSA:3.30.360.10	Dihydrodipicolinate Reductase; domain 2
2	337	Hamap	MF_01640	D-erythrose-4-phosphate dehydrogenase [epd].
2	337	InterPro	IPR006422	D-erythrose-4-phosphate dehydrogenase
1	179	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
1	179	InterPro	IPR036291	NAD(P)-binding domain superfamily
4	328	NCBIfam	TIGR01532	erythrose-4-phosphate dehydrogenase
4	328	InterPro	IPR006422	D-erythrose-4-phosphate dehydrogenase
154	318	FunFam	G3DSA:3.30.360.10:FF:000007	D-erythrose-4-phosphate dehydrogenase
3	164	FunFam	G3DSA:3.40.50.720:FF:000001	Glyceraldehyde-3-phosphate dehydrogenase
155	317	SUPERFAMILY	SSF55347	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
1	334	PANTHER	PTHR43148	GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2
1	334	InterPro	IPR020831	Glyceraldehyde/Erythrose phosphate dehydrogenase family
232	249	PRINTS	PR00078	Glyceraldehyde-3-phosphate dehydrogenase signature
232	249	InterPro	IPR020831	Glyceraldehyde/Erythrose phosphate dehydrogenase family
176	192	PRINTS	PR00078	Glyceraldehyde-3-phosphate dehydrogenase signature
176	192	InterPro	IPR020831	Glyceraldehyde/Erythrose phosphate dehydrogenase family
112	125	PRINTS	PR00078	Glyceraldehyde-3-phosphate dehydrogenase signature
112	125	InterPro	IPR020831	Glyceraldehyde/Erythrose phosphate dehydrogenase family
149	167	PRINTS	PR00078	Glyceraldehyde-3-phosphate dehydrogenase signature
149	167	InterPro	IPR020831	Glyceraldehyde/Erythrose phosphate dehydrogenase family
272	287	PRINTS	PR00078	Glyceraldehyde-3-phosphate dehydrogenase signature
272	287	InterPro	IPR020831	Glyceraldehyde/Erythrose phosphate dehydrogenase family

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

0.685

Likely same site as FPocket 8 2.6 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.04

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Surrounding area

Pocket 3 P2Rank #3

0.025

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Surrounding area

Pocket 4 P2Rank #4

0.013

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Surrounding area

Pocket 5 P2Rank #5

0.011

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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 #8

0.7

Likely same site as P2Rank 1 2.6 Å 15 shared residues 94% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:155-155 Nucleophile

UniProt: Binding site:12-13

UniProt: Binding site:123-123

UniProt: Binding site:154-156

UniProt: Binding site:200-200

UniProt: Binding site:213-214

UniProt: Binding site:236-236

UniProt: Binding site:318-318

UniProt: Site:182-182 Activates thiol group during catalysis

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.769

Likely same site as FPocket 3 2.5 Å 18 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.056

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Surrounding area

Pocket 3 P2Rank #3

0.021

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Surrounding area

Pocket 4 P2Rank #4

0.017

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Surrounding area

Pocket 5 P2Rank #5

0.014

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Surrounding area

Residue sets

UniProt: Active site:155-155 Nucleophile

UniProt: Binding site:12-13

UniProt: Binding site:123-123

UniProt: Binding site:154-156

UniProt: Binding site:200-200

UniProt: Binding site:213-214

UniProt: Binding site:236-236

UniProt: Binding site:318-318

UniProt: Site:182-182 Activates thiol group during catalysis

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_A0A0H3GSZ3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4126	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.

60 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 10 records from similar proteins

Structural ligands 8 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3CD PDB via homolog 697.9 Da · LogP -1.69 · TPSA 292.2 Open detail RCSB PDB

AW9 PDB via homolog Detail RCSB PDB

F4F PDB via homolog Detail RCSB PDB

G3H PDB via homolog Detail RCSB PDB

G3P 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
3CD RCSB PDB	2XF8	P0A9B6	697.9 Da LogP -1.69 TPSA 292.2	3 viol.	✓ Clean	`c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P…`
AW9 RCSB PDB	6IQ6	P04406	130.1 Da LogP -0.20 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)C=CC(=O)O`
F4F RCSB PDB	6M61	P04406	282.3 Da LogP 1.60 TPSA 83.8	✓ Ro5	✓ Clean	`CC(C)[C@H]1CC[C@]([C@@H]2[C@@H]1C=C(COC2=O)C(=O…`
G3H RCSB PDB	1NQO	P00362	170.1 Da LogP -1.34 TPSA 104.1	✓ Ro5	✓ Clean	`C([C@H](C=O)O)OP(=O)(O)O`
G3P RCSB PDB	1DC4	P0A9B2	172.1 Da LogP -1.55 TPSA 107.2	✓ Ro5	✓ Clean	`C([C@H](COP(=O)(O)O)O)O`
MLI RCSB PDB	6GFP	Q8DIW5	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
PHN RCSB PDB	5TSO	P00355	180.2 Da LogP 2.78 TPSA 25.8	✓ Ro5	✓ Clean	`c1cc2ccc3cccnc3c2nc1`
XPE RCSB PDB	6YND	P04406	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`C(COCCOCCOCCOCCOCCOCCOCCOCCOCCO)O`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL3559427 ChEMBL	P04406	7.00 ~100.0 nM	936.8 Da LogP 0.98 TPSA 325.2	3 viol.	✓ Clean	`COc1cccc(C(=O)NC2C(O)[C@@H](COP(=O)([O-])OP(=O)…`
CHEMBL3585922 ChEMBL	P04406	—	280.3 Da LogP 1.62 TPSA 76.1	✓ Ro5	✓ Clean	`CC(C)[C@H]1CC[C@@]2(CO2)[C@H]2C(=O)OCC(C(=O)O)=…`

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
ZINC12501520 ZINC	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC15272438 ZINC	1.000	280.3 Da LogP 1.62 TPSA 76.1	✓ Ro5	✓ Clean	`CC(C)[C@@H]1CC[C@]2(CO2)[C@H]2C(=O)OCC(C(=O)O)=…`
ZINC257452854 ZINC	1.000	280.3 Da LogP 1.62 TPSA 76.1	✓ Ro5	✓ Clean	`CC(C)[C@@H]1CC[C@]2(CO2)[C@H]2C(=O)OCC(C(=O)O)=…`
ZINC257452855 ZINC	1.000	280.3 Da LogP 1.62 TPSA 76.1	✓ Ro5	✓ Clean	`CC(C)[C@@H]1CC[C@]2(CO2)[C@@H]2C(=O)OCC(C(=O)O)…`
ZINC3874716 ZINC	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769 ZINC	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5761434 ZINC	1.000	280.3 Da LogP 1.62 TPSA 76.1	✓ Ro5	✓ Clean	`CC(C)[C@H]1CC[C@@]2(CO2)[C@H]2C(=O)OCC(C(=O)O)=…`
ZINC85550763 ZINC	1.000	280.3 Da LogP 1.62 TPSA 76.1	✓ Ro5	✓ Clean	`CC(C)[C@@H]1CC[C@]2(CO2)[C@@H]2C(=O)OCC(C(=O)O)…`
ZINC238950253 ZINC	0.756	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950256 ZINC	0.756	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950259 ZINC	0.756	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950261 ZINC	0.756	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC231965 ZINC	0.696	214.7 Da LogP 3.44 TPSA 25.8	✓ Ro5	✓ Clean	`Clc1ccc2ccc3cccnc3c2n1`
ZINC40442691 ZINC	0.696	259.1 Da LogP 3.55 TPSA 25.8	✓ Ro5	✓ Clean	`Brc1ccc2ccc3cccnc3c2n1`
ZINC115086873 ZINC	0.688	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC137432264 ZINC	0.688	457.6 Da LogP -0.91 TPSA 129.3	1 viol.	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC146143823 ZINC	0.688	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1542984442 ZINC	0.688	413.5 Da LogP -0.93 TPSA 120.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1565503710 ZINC	0.688	254.3 Da LogP -0.03 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCS`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792028 ZINC	0.688	430.6 Da LogP 0.04 TPSA 94.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC1857792057 ZINC	0.688	474.6 Da LogP 0.06 TPSA 103.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC230494776 ZINC	0.688	325.4 Da LogP -0.96 TPSA 101.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38917157 ZINC	0.688	210.3 Da LogP -0.04 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCS`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5650743 ZINC	0.688	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC77271182 ZINC	0.688	281.3 Da LogP -0.98 TPSA 92.4	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCO`
ZINC83253921 ZINC	0.688	369.5 Da LogP -0.95 TPSA 110.9	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC90741446 ZINC	0.688	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447 ZINC	0.688	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`
ZINC144169243 ZINC	0.647	281.3 Da LogP -1.37 TPSA 89.4	✓ Ro5	✓ Clean	`OCCOCCOCCNCCOCCOCCO`
ZINC205758716 ZINC	0.647	457.6 Da LogP -1.31 TPSA 126.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCNCCOCCOCCOCCOCCO`
ZINC575441396 ZINC	0.647	369.5 Da LogP -1.34 TPSA 107.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCNCCOCCOCCOCCO`
ZINC12360002 ZINC	0.644	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.644	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.644	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.644	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC53683898 ZINC	0.644	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.644	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.644	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586022 ZINC	0.644	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`

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.

erythrose-4-phosphate dehydrogenase

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

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways