Protein profile

PA4400

hypothetical protein

Genome: NC_002516.2

Gene: PA4400 Structure source: AlphaFold UniProt Q9HW06

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Amino acids 315

Annotations 10

Features 32

PDB binders 6

Druggability 0.613

Overview

Basic information about this protein and its source genome.

Accession: PA4400
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4400
Status: annotated
Amino acids: 315
Structure source: AlphaFold

3.6.1.55

GO:0035539 Catalysis of the reaction: 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate (8-oxo-dGTP) + H2O = 8-oxo-7,8-dihydrodeoxyguanosine phosphate (8-oxo-dGMP) + diphosphate. 8-oxo-dGTP is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for DNA synthesis causing transversion mutations. 8-oxo-dGTPase hydrolyses 8-oxo-dGTP to its monophosphate form to prevent the misincorporation of 8-oxo-dGTP into cellular DNA. GO:0008413 Catalysis of the reaction: 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) + H2O = 8-oxo-7,8-dihydroguanosine diphosphate (8-oxo-GDP) + phosphate. 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for transcription. GO:0044715 Catalysis of the reaction 8-oxo-dGDP + H2O = 8-oxo-dGMP + phosphate. GO:0044716 Catalysis of the reaction 8-oxo-GDP + H2O = 8-oxo-GMP + phosphate. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. GO:0046872 Binding to a metal ion.

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 0.613

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

3.6.1.55

Gene Ontology (GO)

GO:0035539 Catalysis of the reaction: 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate (8-oxo-dGTP) + H2O = 8-oxo-7,8-dihydrodeoxyguanosine phosphate (8-oxo-dGMP) + diphosphate. 8-oxo-dGTP is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for DNA synthesis causing transversion mutations. 8-oxo-dGTPase hydrolyses 8-oxo-dGTP to its monophosphate form to prevent the misincorporation of 8-oxo-dGTP into cellular DNA.
GO:0008413 Catalysis of the reaction: 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) + H2O = 8-oxo-7,8-dihydroguanosine diphosphate (8-oxo-GDP) + phosphate. 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for transcription.
GO:0044715 Catalysis of the reaction 8-oxo-dGDP + H2O = 8-oxo-dGMP + phosphate.
GO:0044716 Catalysis of the reaction 8-oxo-GDP + H2O = 8-oxo-GMP + phosphate.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0046872 Binding to a metal ion.
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:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
GO:0009228 The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
38	59	ProSitePatterns	PS00893	Nudix box signature.
38	59	InterPro	IPR020084	NUDIX hydrolase, conserved site
132	311	CDD	cd00564	TMP_TenI
132	311	InterPro	IPR022998	Thiamine phosphate synthase/TenI
126	313	Gene3D	G3DSA:3.20.20.70	Aldolase class I
126	313	InterPro	IPR013785	Aldolase-type TIM barrel
132	309	Pfam	PF02581	Thiamine monophosphate synthase
132	309	InterPro	IPR022998	Thiamine phosphate synthase/TenI
12	16	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	126	SUPERFAMILY	SSF55811	Nudix
1	126	InterPro	IPR015797	NUDIX hydrolase-like domain superfamily
1	128	FunFam	G3DSA:3.90.79.10:FF:000014	8-oxo-dGTP diphosphatase MutT
2	125	Gene3D	G3DSA:3.90.79.10	Nucleoside Triphosphate Pyrophosphohydrolase
4	11	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	3	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
4	125	CDD	cd03425	MutT_pyrophosphohydrolase
47	62	PRINTS	PR00502	NUDIX hydrolase family signature
47	62	InterPro	IPR020476	NUDIX hydrolase
33	47	PRINTS	PR00502	NUDIX hydrolase family signature
33	47	InterPro	IPR020476	NUDIX hydrolase
1	16	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	125	NCBIfam	TIGR00586	8-oxo-dGTP diphosphatase MutT
1	125	InterPro	IPR003561	Mutator MutT
114	311	SUPERFAMILY	SSF51391	Thiamin phosphate synthase
114	311	InterPro	IPR036206	Thiamin phosphate synthase superfamily
7	124	Pfam	PF14815	NUDIX domain
7	124	InterPro	IPR029119	Adenine DNA glycosylase, C-terminal
17	315	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	128	ProSiteProfiles	PS51462	Nudix hydrolase domain profile.
1	128	InterPro	IPR000086	NUDIX hydrolase domain
2	135	PANTHER	PTHR47707	8-OXO-DGTP DIPHOSPHATASE
2	135	InterPro	IPR047127	Mutator MutT-like

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 PA4400	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				0.613
2				0.398
10				0.258

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.

56 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
523	5ZRO	A0R2K6	482.2 Da LogP -1.46 TPSA 252.0	1 viol.	✓ Clean	`CC1=C(NC(=O)[N+](=C1)[C@H]2C[C@@H]([C@H](O2)CO[…`
8OG	1PPX	P08337	363.2 Da LogP -2.25 TPSA 205.8	1 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C3=C(C(=O)NC(=N3)N)NC2=…`
9L3	5ZRI	A0R2K6	306.2 Da LogP -0.98 TPSA 139.0	✓ Ro5	✓ Clean	`Cc1c[n+](cnc1N)[C@H]2C[C@@H]([C@H](O2)COP(=O)(O…`
APC	1TUM	P08337	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
DCP	5ZRK	A0R2K6	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)CO[P@@](=…`
TLA	3A6S	P08337	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)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
ZINC12503365	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](CO[P@](=O)(O)O[P@…`
ZINC13435050	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC8215945	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)O[P@…`
ZINC13435042	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@](=O)(O)OP(=O…`
ZINC14960508	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](CO[P@](=O)(O)OP(=…`
ZINC142514175	0.818	483.2 Da LogP 0.19 TPSA 233.1	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC12503923	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c…`
ZINC12503924	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532581	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC3645374	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC3861759	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC3869816	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3869817	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3869818	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC71404913	0.804	463.2 Da LogP 0.26 TPSA 209.7	1 viol.	✓ Clean	`C[P@@](=O)(O[P@@](=O)(O)OC[C@H]1O[C@@H](n2ccc(N…`
ZINC71404916	0.804	463.2 Da LogP 0.26 TPSA 209.7	1 viol.	✓ Clean	`C[P@@](=O)(O)O[P@@](C)(=O)O[P@@](=O)(O)OC[C@H]1…`
ZINC8215971	0.796	468.1 Da LogP -1.06 TPSA 244.4	2 viol.	✓ Clean	`O=c1nc(O)ccn1[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC111437949	0.741	481.2 Da LogP -0.72 TPSA 236.2	2 viol.	✓ Clean	`CNc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P…`
ZINC12502055	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC12502057	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12502058	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431057	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431059	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC25726736	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC3861746	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@@](=O)(O)…`
ZINC53683723	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC82142138	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC82142140	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC142487928	0.719	483.2 Da LogP -1.48 TPSA 270.4	2 viol.	✓ Clean	`Nc1nc(=O)n([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)…`
ZINC104864216	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@](=O)(O)OP(=O)(O)O)[C…`
ZINC12504412	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC12504413	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC12504414	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431045	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431047	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC13548733	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC33913782	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC8215624	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC58633440	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC62612120	0.695	481.2 Da LogP -0.87 TPSA 250.2	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC81982895	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC81982899	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC81982903	0.695	482.2 Da LogP -2.25 TPSA 276.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12359024	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1549593	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC5783661	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`

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.