Protein profile

PA3917

molybdopterin converting factor small subunit

Genome: NC_002516.2

Gene: moaD PA3917 Structure source: AlphaFold UniProt Q9HX96

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Amino acids 83

Annotations 3

Features 10

PDB binders 0

Druggability 0.704

Overview

Basic information about this protein and its source genome.

Accession: PA3917
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: moaD PA3917
Status: annotated
Amino acids: 83
Structure source: AlphaFold

GO:1990133 A heterotetrameric protein complex which adenylates two molecules of the sulfur carrier subunit of the molybdopterin cofactor synthase using ATP as part of molybdopterin cofactor (Moco) biosynthesis. In E. coli the subunits are MoeB and MoaD; in human the subunits are MOCS3 and MOCS2A. Moco biosynthesis and its constituent molecules are evolutionarily conserved. GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. 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: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Unknown

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 0.704

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MIRVQYFARYREALGIDGEQLNWDAGLATLGALRQLLVERGGAWERTLGEQNLMCARNQELCGLDEPLQDGDEVAFFPTVTGG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

GO:1990133 A heterotetrameric protein complex which adenylates two molecules of the sulfur carrier subunit of the molybdopterin cofactor synthase using ATP as part of molybdopterin cofactor (Moco) biosynthesis. In E. coli the subunits are MoeB and MoaD; in human the subunits are MOCS3 and MOCS2A. Moco biosynthesis and its constituent molecules are evolutionarily conserved.
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
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.

10 records

Show feature table

Start	End	DB	Term	Name
4	83	Pfam	PF02597	ThiS family
4	83	InterPro	IPR003749	Sulfur carrier ThiS/MoaD-like
1	83	Gene3D	G3DSA:3.10.20.30	-
1	83	InterPro	IPR012675	Beta-grasp domain superfamily
2	83	CDD	cd00754	Ubl_MoaD
1	83	SUPERFAMILY	SSF54285	MoaD/ThiS
1	83	InterPro	IPR016155	Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp
2	83	NCBIfam	TIGR01682	molybdopterin converting factor subunit 1
2	83	PANTHER	PTHR33359	MOLYBDOPTERIN SYNTHASE SULFUR CARRIER SUBUNIT
2	83	InterPro	IPR044672	Molybdopterin synthase sulfur carrier subunit

3D Structure

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

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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 PA3917	AlphaFold	—	—	full sequence	—	Viewing

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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
1				0.704