Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA3623
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3623
Status: annotated
Amino acids: 297
Structure source: AlphaFold

GO

GO:0032153 The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles. GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures. GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: OuterMembrane

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 0.633

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MDKGEGLRLAATLRQWTRLYGGCHLLLGAVVCSLLAACSSSPPGGVKVVDRNGSAPAAARRTPVTSGQYIVRRGDTLYSIAFRFGWDWKALAARNGIAPPYTIQVGQAIQFGGRASTQPSVAKNTPVVAAPVATKPTPVPPAVSTSVPAKPAPAPASTTTPPSSGATPVVAGPAVGGWAWPASGTLIGRFASNGSLNKGIDIAGQLGQPVLAASGGTVVYAGSGLRGYGELVIIKHNETYVSAYGHNRRLLVREGQQVKVGQSIAEMGSTGTDRVKLHFEIRRQGKPVDPLQYLPRR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4

GO:0032153 The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
141	158	MobiDBLite	mobidb-lite	consensus disorder prediction
141	168	MobiDBLite	mobidb-lite	consensus disorder prediction
69	109	Pfam	PF01476	LysM domain
69	109	InterPro	IPR018392	LysM domain
68	294	SUPERFAMILY	SSF51261	Duplicated hybrid motif
68	294	InterPro	IPR011055	Duplicated hybrid motif
99	294	PANTHER	PTHR21666	PEPTIDASE-RELATED
67	107	FunFam	G3DSA:3.10.350.10:FF:000006	YgeR family lipoprotein
1	40	SignalP_EUK	SignalP-noTM	SignalP-noTM
67	111	ProSiteProfiles	PS51782	LysM domain profile.
67	111	InterPro	IPR018392	LysM domain
197	281	CDD	cd12797	M23_peptidase
197	290	Pfam	PF01551	Peptidase family M23
197	290	InterPro	IPR016047	Peptidase M23
69	110	CDD	cd00118	LysM
69	110	InterPro	IPR018392	LysM domain
68	110	Gene3D	G3DSA:3.10.350.10	LysM domain
68	110	InterPro	IPR036779	LysM domain superfamily
68	112	SMART	SM00257	LysM_2
68	112	InterPro	IPR018392	LysM domain
148	295	FunFam	G3DSA:2.70.70.10:FF:000010	M23 family peptidase
152	295	Gene3D	G3DSA:2.70.70.10	Glucose Permease (Domain IIA)
152	295	InterPro	IPR011055	Duplicated hybrid motif

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...

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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 PA3623	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				0.633
3				0.349

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.

22 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
4SQ	4ZYB	O33599	281.2 Da LogP -2.12 TPSA 158.8	✓ Ro5	✓ Clean	`C(CP(=O)(CNC(=O)CN)O)C(=O)NCC(=O)O`
CAC	2B0P	O33599	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
TLA	2B13	O33599	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
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`
ZINC1532740	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`
ZINC3860635	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`
ZINC1560405156	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC2561009	0.571	203.2 Da LogP -2.35 TPSA 121.5	✓ Ro5	✓ Clean	`NCC(=O)NCCC(=O)NCC(=O)O`
ZINC1569725	0.545	246.2 Da LogP -3.62 TPSA 150.6	✓ Ro5	✓ Clean	`NCC(=O)NCC(=O)NCC(=O)NCC(=O)O`
ZINC4545903	0.545	360.3 Da LogP -5.39 TPSA 208.8	1 viol.	✓ Clean	`NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)O`
ZINC4545906	0.545	303.3 Da LogP -4.51 TPSA 179.7	1 viol.	✓ Clean	`NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)O`
ZINC1529331	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@H](C(=O)O)[C@@H](O)C(=O)O`
ZINC1529332	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@H](C(=O)O)[C@H](O)C(=O)O`
ZINC1529333	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@@H](C(=O)O)[C@@H](O)C(=O)O`
ZINC1529334	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@@H](C(=O)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.

PA3623