Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA3918
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: moaC PA3918
Status: annotated
Amino acids: 160
Structure source: AlphaFold

EC

4.6.1.17

GO

GO:0061799 Catalysis of the reaction: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate. 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 51.948
Human E-value: 1.35e-45
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.755

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 2 GO

Enzyme Commission (EC)

1

4.6.1.17

Gene Ontology (GO)

2

GO:0061799 Catalysis of the reaction: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate.
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

13 records

Show feature table

Start	End	DB	Term	Name
1	155	Hamap	MF_01224_B	Cyclic pyranopterin monophosphate synthase [moaC].
1	155	InterPro	IPR047594	Molybdenum cofactor biosynthesis C, bacteria/eukaryotes
1	158	FunFam	G3DSA:3.30.70.640:FF:000001	Cyclic pyranopterin monophosphate synthase
13	151	CDD	cd01420	MoaC_PE
13	151	InterPro	IPR047594	Molybdenum cofactor biosynthesis C, bacteria/eukaryotes
9	152	SUPERFAMILY	SSF55040	Molybdenum cofactor biosynthesis protein C, MoaC
9	152	InterPro	IPR036522	Molybdopterin cofactor biosynthesis C (MoaC) domain superfamily
13	147	Pfam	PF01967	MoaC family
13	147	InterPro	IPR002820	Molybdopterin cofactor biosynthesis C (MoaC) domain
1	158	Gene3D	G3DSA:3.30.70.640	Molybdopterin cofactor biosynthesis C (MoaC) domain
1	158	InterPro	IPR036522	Molybdopterin cofactor biosynthesis C (MoaC) domain superfamily
2	149	NCBIfam	TIGR00581	cyclic pyranopterin monophosphate synthase MoaC
2	149	InterPro	IPR023045	Molybdenum cofactor biosynthesis C

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA3918	AlphaFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
5				0.755
2				0.57
3				0.374

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	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	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	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	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.

PA3918