Protein profile

PA3200

hypothetical protein

Genome: NC_002516.2

Gene: PA3200 Structure source: AlphaFold UniProt Q9HZ40

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Amino acids 295

Annotations 3

Features 10

PDB binders 0

Druggability 0.33

Overview

Basic information about this protein and its source genome.

Accession: PA3200
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3200
Status: annotated
Amino acids: 295
Structure source: AlphaFold

GO:0035312 Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of a DNA molecule. GO:0004534 Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of an RNA molecule. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
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 0.33

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

GO:0035312 Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of a DNA molecule.
GO:0004534 Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of an RNA molecule.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Sequence Features

Domain/signature hits from InterPro and related databases.

10 records

Show feature table

Start	End	DB	Term	Name
1	261	PANTHER	PTHR42924	EXONUCLEASE
1	276	SUPERFAMILY	SSF89550	PHP domain-like
1	276	InterPro	IPR016195	Polymerase/histidinol phosphatase-like
3	253	CDD	cd07438	PHP_HisPPase_AMP
4	66	Pfam	PF02811	PHP domain
4	66	InterPro	IPR004013	PHP domain
96	172	Gene3D	G3DSA:1.10.150.650	-
3	253	Gene3D	G3DSA:3.20.20.140	-
3	68	SMART	SM00481	npolultra
3	68	InterPro	IPR003141	Polymerase/histidinol phosphatase, N-terminal

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 PA3200	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
2				0.33
4				0.258