Protein profile

PA5345

ATP-dependent DNA helicase RecG

Genome: NC_002516.2

Gene: recG PA5345 Structure source: AlphaFold UniProt Q9HTL3

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Amino acids 691

Annotations 14

Features 34

PDB binders 2

Druggability 0.882

Overview

Basic information about this protein and its source genome.

Accession: PA5345
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: recG PA5345
Status: annotated
Amino acids: 691
Structure source: AlphaFold

5.6.2.4

GO:0043138 Unwinding a DNA helix in the direction 5' to 3', driven by ATP hydrolysis. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis. GO:0009378 Unwinding a DNA helix of DNA containing four-way junctions, including Holliday junctions, driven by ATP hydrolysis.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 24.528
Human E-value: 2.09e-07
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 0.882

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 13 GO

Enzyme Commission (EC)

5.6.2.4

Gene Ontology (GO)

GO:0043138 Unwinding a DNA helix in the direction 5' to 3', driven by ATP hydrolysis.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
GO:0009378 Unwinding a DNA helix of DNA containing four-way junctions, including Holliday junctions, driven by ATP hydrolysis.
GO:0071247 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a chromate stimulus.
GO:0034599 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
GO:0072715 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a selenite ion stimulus.
GO:0034644 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
GO:0006310 Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
GO:0003676 Binding to a nucleic acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
503	587	SMART	SM00490	helicmild6
503	587	InterPro	IPR001650	Helicase, C-terminal
12	170	Pfam	PF17191	RecG wedge domain
12	170	InterPro	IPR033454	RecG, wedge domain
283	447	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
283	447	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
614	675	Pfam	PF19833	ATP-dependent DNA helicase RecG, domain 3, C-terminal
614	675	InterPro	IPR045562	ATP-dependent DNA helicase RecG, domain 3, C-terminal
265	458	SMART	SM00487	ultradead3
265	458	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
45	138	Gene3D	G3DSA:2.40.50.140	-
45	138	InterPro	IPR012340	Nucleic acid-binding, OB-fold
8	671	PANTHER	PTHR47964	ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC
8	671	InterPro	IPR047112	ATP-dependent DNA helicase RecG/Transcription-repair-coupling factor
27	663	NCBIfam	TIGR00643	ATP-dependent DNA helicase RecG
27	663	InterPro	IPR004609	ATP-dependent DNA helicase RecG
7	172	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
7	172	InterPro	IPR012340	Nucleic acid-binding, OB-fold
317	598	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
317	598	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
293	430	Pfam	PF00270	DEAD/DEAH box helicase
293	430	InterPro	IPR011545	DEAD/DEAH box helicase domain
479	586	Pfam	PF00271	Helicase conserved C-terminal domain
479	586	InterPro	IPR001650	Helicase, C-terminal
61	134	CDD	cd04488	RecG_wedge_OBF
456	628	Gene3D	G3DSA:3.40.50.300	-
456	628	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
480	626	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
480	626	InterPro	IPR001650	Helicase, C-terminal
208	448	Gene3D	G3DSA:3.40.50.300	-
208	448	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
45	138	FunFam	G3DSA:2.40.50.140:FF:000351	ATP-dependent DNA helicase RecG
224	451	CDD	cd17992	DEXHc_RecG
456	628	FunFam	G3DSA:3.40.50.300:FF:000391	ATP-dependent DNA helicase RecG

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 PA5345	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
1				0.882
2				0.732
4				0.402

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.

57 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
AGS	6M6B	Q72KB4	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP	6L5N	Q9NR30	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL1471192	P46063	7.25	451.6 Da LogP 1.73 TPSA 104.8	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)NCC(=O)N(CC(=O)NC2CCCCC2)CC2CCC…`
CHEMBL1560762	P46063	6.85	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NCC1CCCO1`
CHEMBL1446521	P46063	6.50	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NCC3CCCO3)n2C)cc1`
CHEMBL1448630	P46063	6.05	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NCC2CCCO2)cc1`
CHEMBL1057	P46063	—	332.3 Da LogP 3.67 TPSA 76.0	✓ Ro5	✓ Clean	`O=C1OC2(c3ccc(O)cc3Oc3cc(O)ccc32)c2ccccc21`

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
ZINC316109	1.000	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NC[C@H]2CCCO2)cc1`
ZINC316110	1.000	294.4 Da LogP 1.48 TPSA 59.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC(=S)NC[C@@H]2CCCO2)cc1`
ZINC3286414	1.000	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)cc1`
ZINC3286415	1.000	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)cc1`
ZINC3860453	1.000	332.3 Da LogP 3.67 TPSA 76.0	✓ Ro5	✓ Clean	`O=C1OC2(c3ccc(O)cc3Oc3cc(O)ccc32)c2ccccc21`
ZINC798668	1.000	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@H]1CCCO1`
ZINC798669	1.000	396.5 Da LogP 1.97 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@@H]1CCC…`
ZINC804908	0.979	382.5 Da LogP 1.58 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCC2)cc1)NC[C@H]1CCCO1`
ZINC804909	0.979	382.5 Da LogP 1.58 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(COc1ccc(S(=O)(=O)NC2CCCC2)cc1)NC[C@@H]1CCCO1`
ZINC3485814	0.870	366.9 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(Cl)cc1`
ZINC3485816	0.870	366.9 Da LogP 2.52 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(Cl)cc1`
ZINC6914139	0.870	350.4 Da LogP 2.01 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(F)cc1`
ZINC6914143	0.870	350.4 Da LogP 2.01 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(F)cc1`
ZINC3402375	0.855	388.5 Da LogP 3.17 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc(C(C)(C)C)c…`
ZINC3402380	0.855	388.5 Da LogP 3.17 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc(C(C)(C)C)…`
ZINC43199396	0.842	331.3 Da LogP 3.54 TPSA 81.8	✓ Ro5	✓ Clean	`Nc1ccc2c(c1)Oc1cc(O)ccc1[C@]21OC(=O)c2ccccc21`
ZINC43199397	0.842	331.3 Da LogP 3.54 TPSA 81.8	✓ Ro5	✓ Clean	`Nc1ccc2c(c1)Oc1cc(O)ccc1[C@@]21OC(=O)c2ccccc21`
ZINC880963	0.839	362.5 Da LogP 1.88 TPSA 78.3	✓ Ro5	✓ Clean	`COc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)cc1`
ZINC880965	0.839	362.5 Da LogP 1.88 TPSA 78.3	✓ Ro5	✓ Clean	`COc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)cc1`
ZINC12360002	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC2207000	0.810	403.5 Da LogP 2.22 TPSA 98.1	✓ Ro5	✓ Clean	`CCC(=O)Nc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2C)c…`
ZINC2207001	0.810	403.5 Da LogP 2.22 TPSA 98.1	✓ Ro5	✓ Clean	`CCC(=O)Nc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2C)…`
ZINC31977053	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC3286424	0.786	422.6 Da LogP 3.94 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@H]3CCCO3)n2-c2ccc(C)c…`
ZINC3286426	0.786	422.6 Da LogP 3.94 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccc(-c2nnc(SCC(=O)NC[C@@H]3CCCO3)n2-c2ccc(C)…`
ZINC15020070	0.780	346.3 Da LogP 3.97 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc2c(c1)Oc1cc(O)ccc1[C@@]21OC(=O)c2ccccc21`
ZINC15020073	0.780	346.3 Da LogP 3.97 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc2c(c1)Oc1cc(O)ccc1[C@]21OC(=O)c2ccccc21`
ZINC9193273	0.780	386.5 Da LogP 2.75 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1ccc2c(c1)CCCC2`
ZINC9193274	0.780	386.5 Da LogP 2.75 TPSA 69.0	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1ccc2c(c1)CCCC2`
ZINC335097	0.778	235.3 Da LogP 1.60 TPSA 47.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC[C@H]2CCCO2)cc1`
ZINC335098	0.778	235.3 Da LogP 1.60 TPSA 47.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NC[C@@H]2CCCO2)cc1`
ZINC301598	0.766	278.4 Da LogP 1.78 TPSA 50.4	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)NC(=S)NC[C@H]2CCCO2)cc1`
ZINC301599	0.766	278.4 Da LogP 1.78 TPSA 50.4	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)NC(=S)NC[C@@H]2CCCO2)cc1`
ZINC14183634	0.763	333.4 Da LogP 1.26 TPSA 81.9	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@@H]2CCCO2)nnc1-c1cccnc1`
ZINC14183635	0.763	333.4 Da LogP 1.26 TPSA 81.9	✓ Ro5	✓ Clean	`Cn1c(SCC(=O)NC[C@H]2CCCO2)nnc1-c1cccnc1`
ZINC5861269	0.754	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccccc1-c1nnc(SCC(=O)NC[C@@H]2CCCO2)n1C`
ZINC5861281	0.754	346.5 Da LogP 2.18 TPSA 69.0	✓ Ro5	✓ Clean	`Cc1ccccc1-c1nnc(SCC(=O)NC[C@H]2CCCO2)n1C`
ZINC358808	0.750	320.5 Da LogP 2.77 TPSA 50.4	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C(=O)NC(=S)NC[C@H]2CCCO2)cc1`
ZINC358809	0.750	320.5 Da LogP 2.77 TPSA 50.4	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C(=O)NC(=S)NC[C@@H]2CCCO2)cc1`
ZINC798730	0.745	356.4 Da LogP 1.05 TPSA 93.7	✓ Ro5	✓ Clean	`CC(C)NS(=O)(=O)c1ccc(OCC(=O)NC[C@H]2CCCO2)cc1`
ZINC810030	0.745	394.5 Da LogP 2.53 TPSA 84.5	✓ Ro5	✓ Clean	`O=C(CCc1ccc(S(=O)(=O)NC2CCCCC2)cc1)NC[C@H]1CCCO1`

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.