Protein target profile

KP13_03039

Molybdenum cofactor biosynthesis protein C

Genome: KpKP13 Gene: AHE45575.1 moaC 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GQ77

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Length 162

Pocket druggability 0.472

Direct ligand evidence 0 5 total records

Functional annotation 1 EC 2 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.47. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.52. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

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 (%): 48.366 Lower values reduce human off-target concern.
Human E-value: 3.48e-42
Gut microbiome similarity: 16.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 56.129 Higher values support similarity to known essential genes.
DEG E-value: 2.33e-53 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 93.71 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.472

Structure A0A0H3GQ77

Pocket Pocket 8

P2Rank 0.515

Structure A0A0H3GQ77

Pocket Pocket 1

ColabFold model

FPocket 0.448 · Pocket 5

P2Rank 0.566 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 800 / 4744 genomes with a hit

Prevalence 16.9%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GQ77

Sequence

Primary amino-acid sequence viewer.

MSQLTHINAAGEAHMVDVSGKAETVREARAEAYVEMQATTLAMIIDGSHHKGDVFATARIAGIQAAKRTWELIPLCHPLMLSKVEVNLQAQPEHNRVRIESLCRLTGKTGVEMEALTAASVAALTIYDMCKAVQKDMVIGPVRLLAKSGGKSGDFKVGECHD

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 2 GO

Enzyme Commission (EC)

4.6.1.17

Gene Ontology (GO)

GO:0006777 The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
GO:0061799 Catalysis of the reaction: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

13 records

Show feature table

Start	End	DB	Term	Name
1	162	FunFam	G3DSA:3.30.70.640:FF:000001	Cyclic pyranopterin monophosphate synthase
15	154	CDD	cd01420	MoaC_PE
15	154	InterPro	IPR047594	Molybdenum cofactor biosynthesis C, bacteria/eukaryotes
1	160	Gene3D	G3DSA:3.30.70.640	Molybdopterin cofactor biosynthesis C (MoaC) domain
1	160	InterPro	IPR036522	Molybdopterin cofactor biosynthesis C (MoaC) domain superfamily
15	150	Pfam	PF01967	MoaC family
15	150	InterPro	IPR002820	Molybdopterin cofactor biosynthesis C (MoaC) domain
2	158	Hamap	MF_01224_B	Cyclic pyranopterin monophosphate synthase [moaC].
2	158	InterPro	IPR047594	Molybdenum cofactor biosynthesis C, bacteria/eukaryotes
4	152	NCBIfam	TIGR00581	cyclic pyranopterin monophosphate synthase MoaC
4	152	InterPro	IPR023045	Molybdenum cofactor biosynthesis C
11	155	SUPERFAMILY	SSF55040	Molybdenum cofactor biosynthesis protein C, MoaC
11	155	InterPro	IPR036522	Molybdopterin cofactor biosynthesis C (MoaC) domain superfamily

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 · FPocket

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

Site 1 FPocket #8

0.472

Likely same site as P2Rank 1 6.3 Å 5 shared residues 83% of smaller site

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Surrounding area

Site 2 FPocket #1

0.247

Likely same site as P2Rank 2 2.8 Å 10 shared residues 100% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.515

Likely same site as FPocket 8 6.3 Å 5 shared residues 83% of smaller site

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.017

Likely same site as FPocket 1 2.8 Å 10 shared residues 100% of smaller site

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:128-128

UniProt: Binding site:113-114

UniProt: Binding site:75-77

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_A0A0H3GQ77	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_03039	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.

5 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 3 similarity-based ZINC candidates

Best available ligand signal

8CS PDB via homolog 345.2 Da · LogP -1.63 · TPSA 177.9 Open detail RCSB PDB

FLC PDB via homolog Detail RCSB PDB

ZINC34962340 ZINC proposed compound · Tanimoto 0.639 Detail ZINC

ZINC59066352 ZINC proposed compound · Tanimoto 0.639 Detail ZINC

ZINC59066358 ZINC proposed compound · Tanimoto 0.639 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
8CS RCSB PDB	4PYD	P0A738	345.2 Da LogP -1.63 TPSA 177.9	✓ Ro5	✓ Clean	`C1[C@@H]2[C@@H](C(=O)[C@H]3[C@@H](O2)NC4=C(N3)C…`
FLC RCSB PDB	2EKN	O59475	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=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
ZINC34962340 ZINC	0.639	363.2 Da LogP -2.52 TPSA 201.3	2 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@@H]1[C@H](N2)O[C@@H]2CO[…`
ZINC59066352 ZINC	0.639	363.2 Da LogP -2.52 TPSA 201.3	2 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H]1[C@H](N2)O[C@@H]2CO[P…`
ZINC59066358 ZINC	0.639	363.2 Da LogP -2.52 TPSA 201.3	2 viol.	✓ Clean	`Nc1nc2c(c(=O)[nH]1)N[C@H]1[C@H](N2)O[C@@H]2CO[P…`

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.