KpATCC43816 Protein target profile

mannose-6-phosphate isomerase, class I

Accession: VK055_0991

Gene: AIK79614.1 manA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3GS87

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Length 392

Pocket druggability (P2Rank · AlphaFold DB model) 0.834

Metabolic reactions 3

Chokepoint Yes

Direct ligand evidence 0 52 total records

Functional annotation 1 EC 5 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

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.83. Structure available AlphaFold DB model + ColabFold model 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 (%): 39.791 Lower values reduce human off-target concern.
Human E-value: 1.47e-29
Gut microbiome similarity: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 79.795 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.85 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) 0.834

Structure A0A0H3GS87

Pocket Pocket 1

Druggability (FPocket) 0.226

Structure A0A0H3GS87

Pocket Pocket 9

ColabFold model

P2Rank 0.801 · Pocket 1

FPocket 0.281 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 107 / 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

Attractive metabolic target: catalyzes a consuming chokepoint reaction in Amino sugar and nucleotide sugar metabolism.

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

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MQKLINAVQNYAWGSHTALTELYGIANPDNLPMAELWMGAHPKSSSQILAADGQPRSLREVIDADKAALLGDKVAARFGELPFLFKVLCAAQPLSIQVHPNKQASEEGFARENAAGIPLSAAERNYKDPNHKPELVFALTPFLAMNAFREFSEIVTLLQPVASAHPAIGAFLQQPDATHLSQLFASLLNMQGEEKAKALQVLRDVLAREQGEPWQTIRLIAEFYPDDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPAGELLTQPQRHGAELDFPIPVEDFAFSLHDLSAEASDLAQASAAIVFCVDGEAVLRKGDQSLTLKPGESAFVAASESPVQVSGRGRVARVFNKLQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

5.3.1.8

Gene Ontology (GO)

GO:0008270 Binding to a zinc ion (Zn).
GO:0009298 The chemical reactions and pathways resulting in the formation of GDP-mannose, a substance composed of mannose in glycosidic linkage with guanosine diphosphate.
GO:0004476 Catalysis of the reaction: D-mannose 6-phosphate = D-fructose 6-phosphate.
GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

41 records

Show feature table

Start	End	DB	Term	Name
301	382	Gene3D	G3DSA:2.60.120.10	Jelly Rolls
301	382	InterPro	IPR014710	RmlC-like jelly roll fold
2	380	PANTHER	PTHR10309	MANNOSE-6-PHOSPHATE ISOMERASE
2	380	InterPro	IPR016305	Mannose-6-phosphate isomerase
4	382	NCBIfam	TIGR00218	mannose-6-phosphate isomerase, class I
4	382	InterPro	IPR001250	Mannose-6-phosphate isomerase, type I
1	375	SUPERFAMILY	SSF51182	RmlC-like cupins
1	375	InterPro	IPR011051	RmlC-like cupin domain superfamily
1	150	Pfam	PF20511	Phosphomannose isomerase type I, catalytic domain
1	150	InterPro	IPR046457	Phosphomannose isomerase type I, catalytic domain
4	293	CDD	cd07011	cupin_PMI_type_I_N
1	392	PIRSF	PIRSF001480	PMI
1	392	InterPro	IPR016305	Mannose-6-phosphate isomerase
81	102	PRINTS	PR00714	Phosphomannose isomerase type I signature
81	102	InterPro	IPR016305	Mannose-6-phosphate isomerase
255	274	PRINTS	PR00714	Phosphomannose isomerase type I signature
255	274	InterPro	IPR016305	Mannose-6-phosphate isomerase
274	293	PRINTS	PR00714	Phosphomannose isomerase type I signature
274	293	InterPro	IPR016305	Mannose-6-phosphate isomerase
126	149	PRINTS	PR00714	Phosphomannose isomerase type I signature
126	149	InterPro	IPR016305	Mannose-6-phosphate isomerase
220	235	PRINTS	PR00714	Phosphomannose isomerase type I signature
220	235	InterPro	IPR016305	Mannose-6-phosphate isomerase
236	255	PRINTS	PR00714	Phosphomannose isomerase type I signature
236	255	InterPro	IPR016305	Mannose-6-phosphate isomerase
32	47	PRINTS	PR00714	Phosphomannose isomerase type I signature
32	47	InterPro	IPR016305	Mannose-6-phosphate isomerase
4	22	PRINTS	PR00714	Phosphomannose isomerase type I signature
4	22	InterPro	IPR016305	Mannose-6-phosphate isomerase
150	300	Gene3D	G3DSA:1.10.441.10	Phosphomannose Isomerase, domain 2
6	275	Gene3D	G3DSA:2.60.120.10	Jelly Rolls
6	275	InterPro	IPR014710	RmlC-like jelly roll fold
5	174	FunFam	G3DSA:2.60.120.10:FF:000030	Mannose-6-phosphate isomerase ManA
255	280	ProSitePatterns	PS00966	Phosphomannose isomerase type I signature 2.
255	280	InterPro	IPR018050	Phosphomannose isomerase, type I, conserved site
157	236	Pfam	PF20512	Phosphomannose isomerase type I, helical insertion domain
157	236	InterPro	IPR046458	Phosphomannose isomerase type I, helical insertion domain
310	357	Pfam	PF01238	Phosphomannose isomerase type I C-terminal
310	357	InterPro	IPR046456	Phosphomannose isomerase type I, C-terminal domain
126	134	ProSitePatterns	PS00965	Phosphomannose isomerase type I signature 1.
126	134	InterPro	IPR018050	Phosphomannose isomerase, type I, conserved site

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

0.834

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Surrounding area

Pocket 2 P2Rank #2

0.072

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Surrounding area

Pocket 3 P2Rank #3

0.06

Likely same site as FPocket 9 1.2 Å 6 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.032

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Surrounding area

Pocket 5 P2Rank #5

0.022

Likely same site as FPocket 9 8.0 Å 2 shared residues 22% of smaller site

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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

0.226

Likely same site as P2Rank 3 1.2 Å 6 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:274-274

UniProt: Binding site:134-134

UniProt: Binding site:255-255

UniProt: Binding site:97-97

UniProt: Binding site:99-99

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.801

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Surrounding area

Pocket 2 P2Rank #2

0.04

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Surrounding area

Pocket 3 P2Rank #3

0.038

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Surrounding area

Pocket 4 P2Rank #4

0.037

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Surrounding area

Pocket 5 P2Rank #5

0.016

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Surrounding area

Residue sets

UniProt: Active site:274-274

UniProt: Binding site:134-134

UniProt: Binding site:255-255

UniProt: Binding site:97-97

UniProt: Binding site:99-99

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_A0A0H3GS87	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0991	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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 2 records from similar proteins

Structural ligands 2 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

9C2 PDB via homolog 260.1 Da · LogP -3.83 · TPSA 182.6 Open detail RCSB PDB

Y1 PDB via homolog Detail RCSB PDB

ZINC12502210 ZINC proposed compound · Tanimoto 0.647 Detail ZINC

ZINC12502212 ZINC proposed compound · Tanimoto 0.647 Detail ZINC

ZINC12502214 ZINC proposed compound · Tanimoto 0.647 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
9C2 RCSB PDB	5NW7	P34948	260.1 Da LogP -3.83 TPSA 182.6	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H](C(=O)NN)O)O)O)OP(=O)(O)O`
Y1 RCSB PDB	3H1W	P25081	88.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Y+2]`

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
ZINC12502210 ZINC	0.647	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@@H](O)COP(=O…`
ZINC12502212 ZINC	0.647	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC12502214 ZINC	0.647	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@@H](O)COP(=…`
ZINC12502216 ZINC	0.647	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@H](O)COP(=O…`
ZINC4523251 ZINC	0.647	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@@H](O)COP(…`
ZINC4523255 ZINC	0.647	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@H](O)COP(=…`
ZINC4523257 ZINC	0.647	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@@H](O)COP(=…`
ZINC4523259 ZINC	0.647	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@H](O)COP(=O…`
ZINC100065511 ZINC	0.600	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC100085043 ZINC	0.600	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC104869937 ZINC	0.600	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC13537943 ZINC	0.600	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC85994845 ZINC	0.600	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC12501558 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(…`
ZINC12501560 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O…`
ZINC12501562 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)…`
ZINC12501564 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(…`
ZINC1532623 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(…`
ZINC2047359 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)COP(=O…`
ZINC2545091 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O…`
ZINC3869602 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)COP(=…`
ZINC3869603 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)COP(=O…`
ZINC3869604 ZINC	0.571	276.1 Da LogP -3.38 TPSA 185.0	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC5830339 ZINC	0.571	231.1 Da LogP -2.68 TPSA 156.5	1 viol.	✓ Clean	`O=C(NO)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3870277 ZINC	0.543	310.1 Da LogP -2.50 TPSA 191.0	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC5132038 ZINC	0.541	290.2 Da LogP -3.90 TPSA 185.0	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC2516111 ZINC	0.529	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)CO`
ZINC2522704 ZINC	0.529	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC3869812 ZINC	0.529	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC4887586 ZINC	0.528	260.1 Da LogP -2.35 TPSA 164.8	1 viol.	✓ Clean	`O=C(O)C[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC4887587 ZINC	0.528	260.1 Da LogP -2.35 TPSA 164.8	1 viol.	✓ Clean	`O=C(O)C[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC4887588 ZINC	0.528	260.1 Da LogP -2.35 TPSA 164.8	1 viol.	✓ Clean	`O=C(O)C[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC4887589 ZINC	0.528	260.1 Da LogP -2.35 TPSA 164.8	1 viol.	✓ Clean	`O=C(O)C[C@@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC100657408 ZINC	0.514	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC215934438 ZINC	0.514	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC255961849 ZINC	0.514	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC255961850 ZINC	0.514	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC5132021 ZINC	0.514	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1529626 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC1530556 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532567 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532851 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC167996807 ZINC	0.500	301.2 Da LogP -3.12 TPSA 173.6	1 viol.	✓ Clean	`CC(=O)N[C@@H](C=O)[C@@H](O)[C@@H](O)[C@H](O)COP…`
ZINC22116391 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC30320708 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC3606137 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3869426 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC5167283 ZINC	0.500	301.2 Da LogP -3.12 TPSA 173.6	1 viol.	✓ Clean	`CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)COP(…`
ZINC8551307 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC8551308 ZINC	0.500	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(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 A0A0H3GS87

Pathways

BioCyc MANNPISOM-RXN-CPD-15711//FRUCTOSE-6P.23. BioCyc MANNPISOM-RXN-MANNOSE-6P//FRUCTOSE-6P.24. KEGG R00772 BioCyc MANNPISOM-RXN