Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA3257
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: prc PA3257
Status: annotated
Amino acids: 698
Structure source: AlphaFold

GO

GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. GO:0005515 Binding to a protein.

Target profile

Computed evidence for target prioritization.

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

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 0.623

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6

GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
GO:0004175 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
GO:0005515 Binding to a protein.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
8	23	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	7	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
253	330	SMART	SM00228	pdz_new
253	330	InterPro	IPR001478	PDZ domain
606	640	Coils	Coil	Coil
253	350	Gene3D	G3DSA:2.30.42.10	-
253	350	InterPro	IPR036034	PDZ superfamily
24	32	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
244	328	SUPERFAMILY	SSF50156	PDZ domain-like
244	328	InterPro	IPR036034	PDZ superfamily
646	676	MobiDBLite	mobidb-lite	consensus disorder prediction
1	25	SignalP_EUK	SignalP-noTM	SignalP-noTM
252	337	CDD	cd00988	PDZ_CTP_protease
210	565	NCBIfam	TIGR00225	C-terminal processing peptidase
210	565	InterPro	IPR004447	C-terminal-processing peptidase S41A
336	545	SMART	SM00245	tsp_4
336	545	InterPro	IPR005151	Tail specific protease
188	549	SUPERFAMILY	SSF52096	ClpP/crotonase
188	549	InterPro	IPR029045	ClpP/crotonase-like domain superfamily
176	262	FunFam	G3DSA:3.30.750.44:FF:000007	Periplasmic tail-specific protease
52	239	Pfam	PF17804	Tail specific protease N-terminal domain
52	239	InterPro	IPR040573	Tail specific protease, N-terminal domain
370	543	Pfam	PF03572	Peptidase family S41
370	543	InterPro	IPR005151	Tail specific protease
33	698	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
253	350	FunFam	G3DSA:2.30.42.10:FF:000162	Tail-specific protease
370	542	CDD	cd07560	Peptidase_S41_CPP
370	542	InterPro	IPR004447	C-terminal-processing peptidase S41A
351	542	Gene3D	G3DSA:3.90.226.10	-
1	32	Phobius	SIGNAL_PEPTIDE	Signal peptide region
549	689	Pfam	PF11818	C-terminal domain of tail specific protease (DUF3340)
549	689	InterPro	IPR020992	Tail specific protease, C-terminal
1	23	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
335	564	FunFam	G3DSA:3.90.226.10:FF:000090	Tail-specific protease
195	215	Coils	Coil	Coil
177	520	Gene3D	G3DSA:3.30.750.44	-
246	326	Pfam	PF00595	PDZ domain
246	326	InterPro	IPR001478	PDZ domain
641	677	MobiDBLite	mobidb-lite	consensus disorder prediction
157	568	PANTHER	PTHR32060	TAIL-SPECIFIC PROTEASE
1	32	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
245	315	ProSiteProfiles	PS50106	PDZ domain profile.
245	315	InterPro	IPR001478	PDZ domain

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 PA3257	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
3				0.623
7				0.233

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.

1 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
TMO	6VBB	A0A1E3M7A1	75.1 Da LogP 0.19 TPSA 23.1	✓ Ro5	✓ Clean	`C[N+](C)(C)[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).

No virtual-screening candidates for this protein.

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.

PA3257