Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA1770
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA1770 ppsA
Status: annotated
Amino acids: 791
Structure source: AlphaFold

EC

2.7.9.2

GO

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0046872 Binding to a metal ion. GO:0008986 Catalysis of the reaction: ATP + H2O + pyruvate = AMP + 2 H+ + phosphate + phosphoenolpyruvate. GO:0006094 The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol. 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. GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
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 0.545

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)

1

2.7.9.2

Gene Ontology (GO)

9

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0046872 Binding to a metal ion.
GO:0008986 Catalysis of the reaction: ATP + H2O + pyruvate = AMP + 2 H+ + phosphate + phosphoenolpyruvate.
GO:0006094 The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
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.
GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
GO:0006090 The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.
GO:0016310 The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

Sequence Features

Domain/signature hits from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
477	787	Gene3D	G3DSA:3.20.20.60	-
477	787	InterPro	IPR040442	Pyruvate kinase-like domain superfamily
693	711	ProSitePatterns	PS00742	PEP-utilizing enzymes signature 2.
693	711	InterPro	IPR023151	PEP-utilising enzyme, conserved site
1	384	SUPERFAMILY	SSF56059	Glutathione synthetase ATP-binding domain-like
193	356	Gene3D	G3DSA:3.30.470.20	-
413	424	ProSitePatterns	PS00370	PEP-utilizing enzymes phosphorylation site signature.
413	424	InterPro	IPR018274	PEP-utilising enzyme, active site
358	476	FunFam	G3DSA:3.50.30.10:FF:000002	Phosphoenolpyruvate synthase
193	356	FunFam	G3DSA:3.30.470.20:FF:000017	Phosphoenolpyruvate synthase
17	342	Pfam	PF01326	Pyruvate phosphate dikinase, AMP/ATP-binding domain
17	342	InterPro	IPR002192	Pyruvate phosphate dikinase, AMP/ATP-binding
1	192	FunFam	G3DSA:3.30.1490.20:FF:000010	Phosphoenolpyruvate synthase
358	476	Gene3D	G3DSA:3.50.30.10	Phosphohistidine domain
383	454	Pfam	PF00391	PEP-utilising enzyme, mobile domain
383	454	InterPro	IPR008279	PEP-utilising enzyme, mobile domain
693	708	PRINTS	PR01736	Phosphoenolpyruvate-protein phosphotransferase signature
746	758	PRINTS	PR01736	Phosphoenolpyruvate-protein phosphotransferase signature
710	725	PRINTS	PR01736	Phosphoenolpyruvate-protein phosphotransferase signature
3	788	PANTHER	PTHR43030	PHOSPHOENOLPYRUVATE SYNTHASE
3	788	InterPro	IPR006319	Phosphoenolpyruvate synthase
5	786	NCBIfam	TIGR01418	pyruvate, water dikinase
5	786	InterPro	IPR006319	Phosphoenolpyruvate synthase
481	780	Pfam	PF02896	PEP-utilising enzyme, PEP-binding domain
481	780	InterPro	IPR000121	PEP-utilising enzyme, C-terminal
347	464	SUPERFAMILY	SSF52009	Phosphohistidine domain
347	464	InterPro	IPR036637	Phosphohistidine domain superfamily
2	192	Gene3D	G3DSA:3.30.1490.20	-
2	192	InterPro	IPR013815	ATP-grasp fold, subdomain 1
1	791	PIRSF	PIRSF000854	PEP_synthase
1	791	InterPro	IPR006319	Phosphoenolpyruvate synthase
461	786	SUPERFAMILY	SSF51621	Phosphoenolpyruvate/pyruvate domain
461	786	InterPro	IPR015813	Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
477	788	FunFam	G3DSA:3.20.20.60:FF:000010	Phosphoenolpyruvate synthase

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...

Legend High Medium Low

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 PA1770	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				0.545
1				0.405

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.

7 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
5WP	5FBU	A0A0X1KHF9	897.0 Da LogP 4.39 TPSA 252.4	3 viol.	✓ Clean	`CCOc1c(c(c2c3c1[C@@H](O/C=C/[C@@H]([C@H]([C@H](…`
NH4	1KBL	P22983	18.0 Da LogP 0.38 TPSA 36.5	✓ Ro5	✓ Clean	`[NH4+]`
OXL	2HWG	P08839	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=O)[O-])[O-]`
PEP	1VBH	P11155	168.0 Da LogP -0.31 TPSA 104.1	✓ Ro5	✓ Clean	`C=C(C(=O)O)OP(=O)(O)O`
PO3	2MP0	P08839	79.0 Da LogP -1.64 TPSA 63.2	✓ Ro5	✓ Clean	`[O-][P-](=O)[O-]`
PPR	1KC7	P22983	168.0 Da LogP -1.18 TPSA 111.9	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)P(=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
ZINC1625170	0.500	235.0 Da LogP 0.94 TPSA 94.8	✓ Ro5	✓ Clean	`O=C(O)C(CP(=O)(O)O)=C(Cl)Cl`

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.

PA1770