KpKP13 Protein target profile

2-hydroxy-3-oxopropionate reductase

Accession: KP13_01072

Gene: AHE42535.1 garR 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GTL6

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Length 302

Pocket druggability (P2Rank · AlphaFold DB model) 0.907

Direct ligand evidence 0 59 total records

Functional annotation 1 EC 6 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

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

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.91. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 9 structural and 0 bioactivity records.

Risks to review

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 (%): 36.842 Lower values reduce human off-target concern.
Human E-value: 1.11e-26
Gut microbiome similarity: 6.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.56 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) 0.907

Structure A0A0H3GTL6

Pocket Pocket 1

Druggability (FPocket) 0.239

Structure A0A0H3GTL6

Pocket Pocket 9

ColabFold model

P2Rank 0.927 · Pocket 1

FPocket 0.789 · Pocket 13

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 283 / 4744 genomes with a hit

Prevalence 6.0%

Sequence

Primary amino-acid sequence viewer.

MKRENIMTIKVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAIAEQCEVIITMLPNSPHVKEVALGENGIIEGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGDIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEVTR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.1.1.60

Gene Ontology (GO)

GO:0008679 Catalysis of the reaction: (R)-glycerate + NADP+ = 2-hydroxy-3-oxopropanoate + NADPH + H+.
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: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:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0046487 The chemical reactions and pathways involving glyoxylate, the anion of glyoxylic acid, HOC-COOH.
GO:0046392 The chemical reactions and pathways resulting in the breakdown of D-galactarate, the anion of galactaric acid.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
9	170	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
9	170	InterPro	IPR036291	NAD(P)-binding domain superfamily
13	26	ProSitePatterns	PS00895	3-hydroxyisobutyrate dehydrogenase signature.
13	26	InterPro	IPR002204	3-hydroxyisobutyrate dehydrogenase-related, conserved site
172	302	FunFam	G3DSA:1.10.1040.10:FF:000008	2-hydroxy-3-oxopropionate reductase
5	171	Gene3D	G3DSA:3.40.50.720	-
10	300	NCBIfam	TIGR01505	2-hydroxy-3-oxopropionate reductase
10	300	InterPro	IPR006398	2-hydroxy-3-oxopropionate reductase
172	289	Pfam	PF14833	NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase
172	289	InterPro	IPR029154	3-hydroxyisobutyrate dehydrogenase-like, NAD-binding domain
7	300	PANTHER	PTHR43060	3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED
7	171	FunFam	G3DSA:3.40.50.720:FF:000071	2-hydroxy-3-oxopropionate reductase
10	169	Pfam	PF03446	NAD binding domain of 6-phosphogluconate dehydrogenase
10	169	InterPro	IPR006115	6-phosphogluconate dehydrogenase, NADP-binding
9	302	Hamap	MF_02032	2-hydroxy-3-oxopropionate reductase [garR].
9	302	InterPro	IPR006398	2-hydroxy-3-oxopropionate reductase
3	301	PIRSF	PIRSF000103	HIBADH
3	301	InterPro	IPR015815	3-hydroxyisobutyrate dehydrogenase-related
170	299	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
170	299	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
172	302	Gene3D	G3DSA:1.10.1040.10	-
172	302	InterPro	IPR013328	6-phosphogluconate dehydrogenase, domain 2

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

0.907

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Surrounding area

Pocket 2 P2Rank #2

0.196

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.017

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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 #9

0.239

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Surrounding area

Residue sets

UniProt: Active site:152-152

UniProt: Binding site:220-220

UniProt: Binding site:77-77

Binding pockets · FPocket

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

Pocket 1 FPocket #13

0.789 Unusual size

Likely same site as P2Rank 1 7.2 Å 24 shared residues 83% of smaller site

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Surrounding area

Pocket 2 FPocket #15

0.236

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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_A0A0H3GTL6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01072	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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3OH PDB via homolog 90.1 Da · LogP -0.55 · TPSA 57.5 Open detail RCSB PDB

7VD PDB via homolog Detail RCSB PDB

9ON PDB via homolog Detail RCSB PDB

AKR PDB via homolog Detail RCSB PDB

BO3 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
3OH RCSB PDB	5Y8O	P9WNY5	90.1 Da LogP -0.55 TPSA 57.5	✓ Ro5	✓ Clean	`C(CO)C(=O)O`
7VD RCSB PDB	5U5G	I6R485	138.1 Da LogP -0.25 TPSA 74.6	✓ Ro5	✓ Clean	`CC(=O)CP(=O)(O)O`
9ON RCSB PDB	5Y8L	P9WNY5	146.1 Da LogP 0.57 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCC(=O)O)C(=O)O`
AKR RCSB PDB	5Y8M	P9WNY5	72.1 Da LogP 0.26 TPSA 37.3	✓ Ro5	✓ Clean	`C=CC(=O)O`
BO3 RCSB PDB	6SM7	P0A9V8	61.8 Da LogP -2.05 TPSA 60.7	✓ Ro5	✓ Clean	`B(O)(O)O`
HIU RCSB PDB	5Y8M	P9WNY5	104.1 Da LogP -0.30 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](CO)C(=O)O`
HUI RCSB PDB	5Y8L	P9WNY5	104.1 Da LogP -0.30 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](CO)C(=O)O`
LLQ RCSB PDB	6SMY	P0A9V8	156.2 Da LogP -1.77 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@@H](CS(=O)(=O)O)O)O`
TLA RCSB PDB	1VPD	Q8ZLV8	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)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).

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
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2029340 ZINC	0.591	216.3 Da LogP 2.38 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029341 ZINC	0.591	216.3 Da LogP 2.38 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@H](CCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029343 ZINC	0.591	216.3 Da LogP 2.38 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCC[C@H](C)C(=O)O)C(=O)O`
ZINC2029346 ZINC	0.591	230.3 Da LogP 2.77 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029348 ZINC	0.591	230.3 Da LogP 2.77 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@H](CCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029350 ZINC	0.591	230.3 Da LogP 2.77 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCC[C@H](C)C(=O)O)C(=O)O`
ZINC2029355 ZINC	0.591	258.4 Da LogP 3.55 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029358 ZINC	0.591	258.4 Da LogP 3.55 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@H](CCCCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC2029360 ZINC	0.591	258.4 Da LogP 3.55 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCCCC[C@H](C)C(=O)O)C(=O)O`
ZINC4100991 ZINC	0.591	286.4 Da LogP 4.33 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC4100995 ZINC	0.591	286.4 Da LogP 4.33 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@H](CCCCCCCCCC[C@@H](C)C(=O)O)C(=O)O`
ZINC4101001 ZINC	0.591	286.4 Da LogP 4.33 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CCCCCCCCCC[C@H](C)C(=O)O)C(=O)O`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC142127993 ZINC	0.571	219.2 Da LogP -1.20 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](O)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC214811896 ZINC	0.571	219.2 Da LogP -1.20 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](O)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC214811946 ZINC	0.571	219.2 Da LogP -1.20 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@H](O)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC214811999 ZINC	0.571	219.2 Da LogP -1.20 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@H](O)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC13529664 ZINC	0.560	320.3 Da LogP -1.08 TPSA 190.3	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)N[C@@H](CCC(=O)O)C(=O)O)C(=…`
ZINC14510370 ZINC	0.556	244.4 Da LogP 3.74 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCO`
ZINC1531061 ZINC	0.556	216.3 Da LogP 2.96 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCO`
ZINC1610426 ZINC	0.556	230.3 Da LogP 3.35 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCO`
ZINC2168567 ZINC	0.556	202.3 Da LogP 2.57 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCO`
ZINC3861297 ZINC	0.556	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCO`
ZINC4284502 ZINC	0.556	258.4 Da LogP 4.13 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCO`
ZINC5287109 ZINC	0.556	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCCO`
ZINC2242980 ZINC	0.552	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC2560662 ZINC	0.552	218.2 Da LogP -1.23 TPSA 129.7	✓ Ro5	✓ Clean	`C[C@@H](N)C(=O)N[C@H](CCC(=O)O)C(=O)O`
ZINC5360219 ZINC	0.552	231.2 Da LogP 0.47 TPSA 103.7	✓ Ro5	✓ Clean	`CC(C)CC(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC3845741 ZINC	0.542	202.2 Da LogP 1.84 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C)[C@@H](CC[C@@H](C)C(=O)O)C(=O)O`
ZINC3845742 ZINC	0.542	202.2 Da LogP 1.84 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C)[C@H](CC[C@@H](C)C(=O)O)C(=O)O`
ZINC3845743 ZINC	0.542	202.2 Da LogP 1.84 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C)[C@@H](CC[C@H](C)C(=O)O)C(=O)O`
ZINC3845744 ZINC	0.542	202.2 Da LogP 1.84 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C)[C@H](CC[C@H](C)C(=O)O)C(=O)O`
ZINC217513646 ZINC	0.538	362.3 Da LogP -1.76 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CC(=O)N[C@@H](CCC(=O)O)C(=O…`
ZINC225956904 ZINC	0.538	362.3 Da LogP -1.76 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CC(=O)N[C@H](CCC(=O)O)C(=O)…`
ZINC225956918 ZINC	0.538	362.3 Da LogP -1.76 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@@H](NC(=O)CC(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC58123315 ZINC	0.538	376.3 Da LogP -1.36 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCC(=O)N[C@@H](CCC(=O)O)C(=…`
ZINC58123320 ZINC	0.538	376.3 Da LogP -1.36 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@H](NC(=O)CCC(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC58123326 ZINC	0.538	376.3 Da LogP -1.36 TPSA 207.4	1 viol.	✓ Clean	`O=C(O)CC[C@@H](NC(=O)CCC(=O)N[C@H](CCC(=O)O)C(=…`
ZINC87491353 ZINC	0.536	259.3 Da LogP -3.16 TPSA 138.5	✓ Ro5	✓ Clean	`O=S(=O)(O)C[C@@H](O)CN(CO)C(CO)CO`
ZINC87491354 ZINC	0.536	259.3 Da LogP -3.16 TPSA 138.5	✓ Ro5	✓ Clean	`O=S(=O)(O)C[C@H](O)CN(CO)C(CO)CO`

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 A0A0H3GTL6