KpATCC43816 Protein target profile

phosphoglucomutase, alpha-D-glucose phosphate-specific

Accession: VK055_1820

Gene: AIK80433.1 pgm 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3GPZ1
Export view
Length 546
Pocket druggability (P2Rank · AlphaFold DB model) 0.66
Metabolic reactions 3
Chokepoint No
Direct ligand evidence 0 7 total records
Functional annotation 1 EC 6 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

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.66, FPocket 0.85). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.85. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.66. Review the complete evidence below

Risks to review

Low human similarity A human hit was flagged, but identity is only 25.843% - a weak match, lower risk than a close homolog. This target also has a predicted binding pocket (P2Rank 0.66) — check the ligand evidence before deprioritizing on off-target risk alone. Microbiome similarity 290 of 4744 screened genomes (6.1%) have a significant similarity hit. This target also has a predicted binding pocket (P2Rank 0.66) — check the ligand evidence before deprioritizing on off-target risk alone.

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 (%)
25.843 Lower values reduce human off-target concern.
Human E-value
2.75e-14
Gut microbiome similarity
6.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

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

Structure confidence

ColabFold pLDDT
97.09 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) 0.66
Structure A0A0H3GPZ1
Pocket Pocket 1
Druggability (FPocket) 0.855
Structure A0A0H3GPZ1
Pocket Pocket 9
ColabFold model
P2Rank 0.675 · Pocket 1
FPocket 0.867 · Pocket 2
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 290 / 4744 genomes with a hit
Prevalence 6.1%

Metabolic context

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

Explore metabolic network
Relative network centrality 0.0% more central than 0.0% of genes in this genome
Chokepoint Not a chokepoint
Pathways
Amino sugar and nucleotide sugar metabolism Galactose metabolism Glycolysis / Gluconeogenesis
Catalyzed reactions

3 reactions mapped to this gene in the metabolic model. Open the full network to see each one, with substrates/products and the reaction-reaction map.

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MAIDKRAGQPAQQSDLINVAQLTAQYYVLKPEVGNAEHAVKFGTSGHRGSAARHNFNEPHILAIAQAIAEDRAKNGITGPCYVGKDTHALSEPAFISVLEVLTANGVDVIVQENNGFTPTPAVSNAILVHNKKGGPLADGIVITPSHNPPEDGGIKYNPPNGGPADTNVTKVVENRANELLAAGLQGVKRISLDAALASGHVKEQDLVQPFIEGLADIVDMAAIQKAGLTLGVDPLGGSGIEYWKRIGEHYKLNLTIVNDQVDQTFRFMHLDKDGAIRMDCSSECAMAGLLALRDKFDLAFANDPDYDRHGIVTPAGLMNPNHYLAVAINYLFQHRPQWGKEVAVGKTLVSSAMIDRVVNDLGRKLVEVPVGFKWFVDGLFDGIFGFGGEESAGASFLRFDGTPWSTDKDGIIMCLLAAEITAVTGKNPQEHYNELAERFGAPSYNRLQASATSAQKAALSKLSPEMVSADTLAGDPITARLTAAPGNGAAIGGLKVMTDNGWFAARPSGTEDAYKIYCESFLGEEHRKLIEKEAVEIVSEVLKNA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization
Cytoplasmic

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0016868 Catalysis of the transfer of a phosphate group from one position to another within a single molecule.
  • GO:0071704 OBSOLETE. The chemical reactions and pathways involving an organic substance, any molecular entity containing carbon.
  • 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:0004614 Catalysis of the reaction: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • 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.

32 records
Show feature table
Start End DB Term Name
443 546 Gene3D G3DSA:3.30.310.50 -
433 544 SUPERFAMILY SSF55957 Phosphoglucomutase, C-terminal domain
433 544 InterPro IPR036900 Alpha-D-phosphohexomutase, C-terminal domain superfamily
12 218 FunFam G3DSA:3.40.120.10:FF:000012 Phosphoglucomutase, alpha-D-glucose phosphate-specific
41 536 PANTHER PTHR22573 PHOSPHOHEXOMUTASE FAMILY MEMBER
41 536 InterPro IPR045244 Phosphoglucomutase
1 544 NCBIfam TIGR01132 phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)
1 544 InterPro IPR005852 Phosphoglucomutase, alpha-D-glucose specific
443 546 FunFam G3DSA:3.30.310.50:FF:000004 Alpha-D-glucose phosphate-specific phosphoglucomutase
210 317 Pfam PF02879 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II
210 317 InterPro IPR005845 Alpha-D-phosphohexomutase, alpha/beta/alpha domain II
319 442 Gene3D G3DSA:3.40.120.10 -
209 317 SUPERFAMILY SSF53738 Phosphoglucomutase, first 3 domains
209 317 InterPro IPR016055 Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III
319 442 FunFam G3DSA:3.40.120.10:FF:000008 Alpha-D-glucose phosphate-specific phosphoglucomutase
40 179 Pfam PF02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I
40 179 InterPro IPR005844 Alpha-D-phosphohexomutase, alpha/beta/alpha domain I
305 446 SUPERFAMILY SSF53738 Phosphoglucomutase, first 3 domains
305 446 InterPro IPR016055 Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III
140 149 ProSitePatterns PS00710 Phosphoglucomutase and phosphomannomutase phosphoserine signature.
140 149 InterPro IPR016066 Alpha-D-phosphohexomutase, conserved site
12 218 Gene3D G3DSA:3.40.120.10 -
20 539 CDD cd05801 PGM_like3
20 539 InterPro IPR005852 Phosphoglucomutase, alpha-D-glucose specific
26 235 SUPERFAMILY SSF53738 Phosphoglucomutase, first 3 domains
26 235 InterPro IPR016055 Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III
480 538 Pfam PF00408 Phosphoglucomutase/phosphomannomutase, C-terminal domain
480 538 InterPro IPR005843 Alpha-D-phosphohexomutase, C-terminal
320 440 Pfam PF02880 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III
320 440 InterPro IPR005846 Alpha-D-phosphohexomutase, alpha/beta/alpha domain III
221 318 Gene3D G3DSA:3.40.120.10 -
221 318 FunFam G3DSA:3.40.120.10:FF:000011 Alpha-D-glucose phosphate-specific phosphoglucomutase

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 · P2Rank

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

Pocket 1 P2Rank #1
0.66
Show in viewer
Surrounding area
Pocket 2 P2Rank #2
0.139
Show in viewer
Surrounding area
Pocket 3 P2Rank #3
0.106
Show in viewer
Surrounding area
Pocket 4 P2Rank #4
0.098
Show in viewer
Surrounding area
Pocket 5 P2Rank #5
0.015
Show in viewer
Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #9
0.855
Show in viewer
Surrounding area
Pocket 2 FPocket #1
0.248 Unusual size
Show in viewer
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_A0A0H3GPZ1
AlphaFold DB — — full sequence — Viewing
ColabFold VK055_1820
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.

7 records
Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records
Transferred evidence 1 records from similar proteins
Structural ligands 1 0 loaded crystals
Measured bioactivity 0 direct and transferred ChEMBL records
Proposed compounds 6 similarity-based ZINC candidates
Best available ligand signal
BTB PDB via homolog 209.2 Da · LogP -3.01 · TPSA 104.4 Open detail RCSB PDB
ZINC1615342 ZINC proposed compound · Tanimoto 1.000 Detail ZINC
ZINC2334905 ZINC proposed compound · Tanimoto 0.522 Detail ZINC
ZINC3159953 ZINC proposed compound · Tanimoto 0.522 Detail ZINC
ZINC5297554 ZINC proposed compound · Tanimoto 0.500 Detail ZINC

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
BTB RCSB PDB
3NA5
Q8ZQW9 209.2 Da LogP -3.01 TPSA 104.4 ✓ Ro5 ✓ Clean C(CO)N(CCO)C(CO)(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 A0A0H3GPZ1

Pathways

KEGG R00959 BioCyc PHOSPHOGLUCMUT-RXN BioCyc PHOSPHOGLUCMUT-RXN-GLC-1-P//ALPHA-GLC-6-P.23. BioCyc PHOSPHOGLUCMUT-RXN-GLC-1-P//GLC-6-P.17.