Protein target profile

PA4446

AlgW protein

Genome: NC_002516.2

Gene: PAERUG_P19_London_7_VIM_2_05_10_06422 PA4446 GUL26_13520 mucD_2 algW CAZ10_21085 3D evidence: Experimental + AlphaFold DB model UniProt Q9HVX1 UniProt A5JJ04

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Length 389

Pocket druggability 0.722

Ligand records 53

EC / GO 0 / 4

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

4 signals

How to read this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal TPW pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Overview

Basic information about this protein and its source genome.

Accession: PA4446
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PAERUG_P19_London_7_VIM_2_05_10_06422 PA4446 GUL26_13520 mucD_2 algW CAZ10_21085
Status: annotated
Amino acids: 389
3D evidence: Experimental + AlphaFold DB model

GO:0008233 Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. GO:0004252 Catalysis of the hydrolysis of internal, alpha-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:0005515 Binding to a protein.

Target profile

Computed evidence for target prioritization.

Human off-target: Hit
Human identity (%): 37.363
Human E-value: 1.72e-19
Gut microbiome off-target: Hit
Essential (DEG): Y
Localization: Unknown

Selected pocket evidence

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.722

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MPKALRFLGWPVLVGVLLALLIIQHNPELVGLPRQEVHVEQAPLLSRLQEGPVSYANAVSRAAPAVANLYTTKMVSKPSHPLFDDPMFRRFFGDNLPQQKRMESSLGSAVIMSAEGYLLTNNHVTAGADQIIVALRDGRETIAQLVGSDPETDLAVLKIDLKNLPAMTLGRSDGIRTGDVCLAIGNPFGVGQTVTMGIISATGRNQLGLNTYEDFIQTDAAINPGNSGGALVDAAGNLIGINTAIFSKSGGSQGIGFAIPTKLALEVMQSIIEHGQVIRGWLGVEVKALTPELAESLGLGETAGIVVAGVYRDGPAARGGLLPGDVILTIDKQEASDGRRSMNQVARTRPGQKISIVVLRNGQKVNLTAEVGLRPPPAPAPQQKQDGGE

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

GO:0008233 Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
GO:0004252 Catalysis of the hydrolysis of internal, alpha-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:0005515 Binding to a protein.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
238	363	SUPERFAMILY	SSF50156	PDZ domain-like
238	363	InterPro	IPR036034	PDZ superfamily
107	241	Pfam	PF13365	Trypsin-like peptidase domain
280	362	SMART	SM00228	pdz_new
280	362	InterPro	IPR001478	PDZ domain
7	24	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
137	157	PRINTS	PR00834	HtrA/DegQ protease family signature
137	157	InterPro	IPR001940	Peptidase S1C
320	332	PRINTS	PR00834	HtrA/DegQ protease family signature
320	332	InterPro	IPR001940	Peptidase S1C
234	251	PRINTS	PR00834	HtrA/DegQ protease family signature
234	251	InterPro	IPR001940	Peptidase S1C
116	128	PRINTS	PR00834	HtrA/DegQ protease family signature
116	128	InterPro	IPR001940	Peptidase S1C
177	201	PRINTS	PR00834	HtrA/DegQ protease family signature
177	201	InterPro	IPR001940	Peptidase S1C
212	229	PRINTS	PR00834	HtrA/DegQ protease family signature
212	229	InterPro	IPR001940	Peptidase S1C
281	370	Pfam	PF13180	PDZ domain
281	370	InterPro	IPR001478	PDZ domain
168	279	FunFam	G3DSA:2.40.10.10:FF:000001	Periplasmic serine protease DegS
32	369	PANTHER	PTHR22939	SERINE PROTEASE FAMILY S1C HTRA-RELATED
51	272	SUPERFAMILY	SSF50494	Trypsin-like serine proteases
51	272	InterPro	IPR009003	Peptidase S1, PA clan
1	31	Phobius	SIGNAL_PEPTIDE	Signal peptide region
278	376	Gene3D	G3DSA:2.30.42.10	-
278	376	InterPro	IPR036034	PDZ superfamily
1	19	SignalP_EUK	SignalP-noTM	SignalP-noTM
280	368	CDD	cd00987	PDZ_serine_protease
262	370	Pfam	PF02163	Peptidase family M50
262	370	InterPro	IPR008915	Peptidase M50
1	11	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
271	362	ProSiteProfiles	PS50106	PDZ domain profile.
271	362	InterPro	IPR001478	PDZ domain
24	31	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
32	389	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
12	23	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
53	274	Gene3D	G3DSA:2.40.10.120	-

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

Loading 3D structure...

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Structural evidence

4 + 1

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 7CO3	X-ray	1.90 Å	A	100.0% 1-389	PDBe RCSB PDBj File	Viewing
PDB 7CO2	X-ray	2.10 Å	A	100.0% 1-389	PDBe RCSB PDBj File	Loaded
PDB 7CO5	X-ray	2.35 Å	B,D,F,H,J,L	96.9% 1-377	PDBe RCSB PDBj File	Loaded
PDB 7CO7	X-ray	2.60 Å	D	84.6% 53-381	PDBe RCSB PDBj File	Loaded
AlphaFold DB PA4446	AlphaFold DB	—	—	full sequence	—	Loaded

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1

0.722

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Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.066

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Site 2 P2Rank #2

0.058

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Site 3 P2Rank #3

0.025

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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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 53 via homologs

Structural ligands 3 0 loaded crystals

Bioactive compounds 0 50 ZINC proposed compounds

Drug-like & clean 52 1 PAINS alerts

Best available ligand signal

CXS PDB via homolog 221.3 Da · LogP 1.19 · TPSA 66.4 Open detail RCSB PDB

Detail RCSB PDB CXS PDB via homolog

Detail RCSB PDB DFP PDB via homolog

Detail RCSB PDB PMS PDB via homolog

Detail ZINC ZINC2004372 ZINC proposed compound · Tanimoto 1.000

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
CXS RCSB PDB	5JD8	A0A5P8YL96	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCCS(=O)(=O)O`
DFP RCSB PDB	3MH5	P0C0V0	166.2 Da LogP 2.23 TPSA 35.5	✓ Ro5	✓ Clean	`CC(C)OP(=O)OC(C)C`
PMS RCSB PDB	6IEO	O06291	172.2 Da LogP 1.07 TPSA 54.4	✓ Ro5	✓ Clean	`c1ccc(cc1)CS(=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
ZINC2004372 ZINC	1.000	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153 ZINC	0.926	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC1710230 ZINC	0.786	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC1764974 ZINC	0.750	266.3 Da LogP 0.46 TPSA 108.7	✓ Ro5	✓ Clean	`O=S(=O)(O)Cc1ccc(CS(=O)(=O)O)cc1`
ZINC389634 ZINC	0.714	246.3 Da LogP 2.80 TPSA 34.1	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)Cc1ccccc1`
ZINC5188799 ZINC	0.630	280.5 Da LogP 4.39 TPSA 24.1	✓ Ro5	✓ Clean	`C(CCCNC1CCCCC1)CCNC1CCCCC1`
ZINC34080186 ZINC	0.609	266.3 Da LogP 0.46 TPSA 108.7	✓ Ro5	✓ Clean	`O=S(=O)(O)Cc1ccccc1CS(=O)(=O)O`
ZINC32210235 ZINC	0.600	251.1 Da LogP 1.84 TPSA 54.4	✓ Ro5	✓ Clean	`O=S(=O)(O)Cc1ccc(Br)cc1`
ZINC1679108 ZINC	0.583	324.4 Da LogP 2.17 TPSA 68.3	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)CS(=O)(=O)Cc1ccccc1`
ZINC163130 ZINC	0.560	232.3 Da LogP 2.66 TPSA 34.1	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)c1ccccc1`
ZINC196676626 ZINC	0.560	340.4 Da LogP 1.14 TPSA 92.3	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)NNS(=O)(=O)Cc1ccccc1`
ZINC399776 ZINC	0.560	336.4 Da LogP 2.69 TPSA 68.3	✓ Ro5	✓ Clean	`O=S(=O)(/C=C/S(=O)(=O)Cc1ccccc1)Cc1ccccc1`
ZINC145170179 ZINC	0.556	250.3 Da LogP 0.48 TPSA 88.5	✓ Ro5	✓ Clean	`CS(=O)(=O)c1ccc(CS(=O)(=O)O)cc1`
ZINC1713408 ZINC	0.556	214.2 Da LogP 0.69 TPSA 71.4	✓ Ro5	✓ Clean	`O=C(O)CS(=O)(=O)Cc1ccccc1`
ZINC255190110 ZINC	0.556	386.5 Da LogP 3.63 TPSA 68.3	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)c1cccc(S(=O)(=O)Cc2ccccc2)c1`
ZINC26478554 ZINC	0.556	200.3 Da LogP 0.59 TPSA 54.4	✓ Ro5	✓ Clean	`O=S(=O)(CCO)Cc1ccccc1`
ZINC35058157 ZINC	0.552	261.3 Da LogP 2.38 TPSA 60.2	✓ Ro5	✓ Clean	`Nc1cccc(CS(=O)(=O)Cc2ccccc2)c1`
ZINC14093286 ZINC	0.538	368.5 Da LogP 1.23 TPSA 92.3	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)NCCNS(=O)(=O)Cc1ccccc1`
ZINC1163467 ZINC	0.536	436.6 Da LogP 4.79 TPSA 68.3	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)c1cccc2c(S(=O)(=O)Cc3ccccc3)c…`
ZINC2509149 ZINC	0.531	211.4 Da LogP 4.27 TPSA 12.0	✓ Ro5	✓ Clean	`CCCCCCCCNC1CCCCC1`
ZINC32929750 ZINC	0.531	289.4 Da LogP 1.90 TPSA 77.2	✓ Ro5	✓ Clean	`NC(=O)c1cccc(CS(=O)(=O)Cc2ccccc2)c1`
ZINC130127586 ZINC	0.529	260.4 Da LogP 1.38 TPSA 58.2	✓ Ro5	✓ Clean	`O=S(=O)(NCCNC1CCCCCC1)C1CC1`
ZINC143515753 ZINC	0.519	200.3 Da LogP 1.64 TPSA 54.4	✓ Ro5	✓ Clean	`CCc1ccccc1CS(=O)(=O)O`
ZINC19367005 ZINC	0.519	224.4 Da LogP 2.83 TPSA 24.1	✓ Ro5	✓ Clean	`C1CCC(NCCNC2CCCCC2)CC1`
ZINC29840 ZINC	0.519	261.3 Da LogP 2.31 TPSA 46.2	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)NCc1ccccc1`
ZINC45069273 ZINC	0.519	273.6 Da LogP 2.93 TPSA 34.1	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)C(Cl)(Cl)Cl`
ZINC12805654 ZINC	0.517	444.6 Da LogP 2.93 TPSA 92.3	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)NCc1cccc(CNS(=O)(=O)Cc2ccccc2…`
ZINC13808031 ZINC	0.517	213.3 Da LogP -0.21 TPSA 98.5	✓ Ro5	✓ Clean	`NC(N)=NS(=O)(=O)Cc1ccccc1`
ZINC1561883 ZINC	0.517	229.3 Da LogP 0.19 TPSA 83.5	✓ Ro5	✓ Clean	`O=C(O)CNS(=O)(=O)Cc1ccccc1`
ZINC1641128 ZINC	0.517	242.3 Da LogP 2.68 TPSA 54.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCCCc1ccccc1`
ZINC17021092 ZINC	0.517	228.3 Da LogP 1.07 TPSA 71.4	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)S(=O)(=O)Cc1ccccc1`
ZINC1704442 ZINC	0.517	228.3 Da LogP 1.07 TPSA 71.4	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)S(=O)(=O)Cc1ccccc1`
ZINC1764786 ZINC	0.517	217.2 Da LogP 0.98 TPSA 97.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(CS(=O)(=O)O)cc1`
ZINC3219150 ZINC	0.517	263.3 Da LogP 2.41 TPSA 57.6	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)N(O)c1ccccc1`
ZINC4512996 ZINC	0.517	228.3 Da LogP 1.08 TPSA 71.4	✓ Ro5	✓ Clean	`O=C(O)CCS(=O)(=O)Cc1ccccc1`
ZINC65593788 ZINC	0.517	274.4 Da LogP 3.42 TPSA 34.1	✓ Ro5	✓ Clean	`Cc1cc(C)cc(CS(=O)(=O)Cc2ccccc2)c1`
ZINC78978926 ZINC	0.516	266.7 Da LogP 3.31 TPSA 34.1	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)c1cccc(Cl)c1`
ZINC96191894 ZINC	0.516	217.2 Da LogP 0.98 TPSA 97.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(CS(=O)(=O)O)c1`
ZINC1641137 ZINC	0.500	222.3 Da LogP 2.23 TPSA 54.4	✓ Ro5	✓ Clean	`O=S(=O)(O)Cc1cccc2ccccc12`
ZINC1672446 ZINC	0.500	228.3 Da LogP 1.49 TPSA 75.3	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC1CCCCC1)C(=O)O`
ZINC1926248 ZINC	0.500	416.5 Da LogP 3.57 TPSA 92.3	✓ Ro5	Alert	`O=S(=O)(Cc1ccccc1)Nc1ccc(NS(=O)(=O)Cc2ccccc2)cc1`
ZINC2168583 ZINC	0.500	237.3 Da LogP 0.16 TPSA 86.6	✓ Ro5	✓ Clean	`O=S(=O)(O)C[C@@H](O)CNC1CCCCC1`
ZINC2168584 ZINC	0.500	237.3 Da LogP 0.16 TPSA 86.6	✓ Ro5	✓ Clean	`O=S(=O)(O)C[C@H](O)CNC1CCCCC1`
ZINC236994621 ZINC	0.500	290.4 Da LogP 0.85 TPSA 75.3	✓ Ro5	✓ Clean	`CCS(=O)(=O)CC(=O)NCCNC1CCCCCC1`
ZINC29852 ZINC	0.500	247.3 Da LogP 2.63 TPSA 46.2	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)Nc1ccccc1`
ZINC399887 ZINC	0.500	274.3 Da LogP 2.48 TPSA 51.2	✓ Ro5	✓ Clean	`O=C(CS(=O)(=O)Cc1ccccc1)c1ccccc1`
ZINC44655186 ZINC	0.500	213.4 Da LogP 3.12 TPSA 21.3	✓ Ro5	✓ Clean	`COCCCCNC1CCCCCCC1`
ZINC5840523 ZINC	0.500	228.3 Da LogP 1.49 TPSA 75.3	✓ Ro5	✓ Clean	`N[C@H](CCCCNC1CCCCC1)C(=O)O`
ZINC65593700 ZINC	0.500	314.3 Da LogP 3.82 TPSA 34.1	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)Cc1cccc(C(F)(F)F)c1`
ZINC728426 ZINC	0.500	351.5 Da LogP 4.22 TPSA 37.4	✓ Ro5	✓ Clean	`O=S(=O)(Cc1ccccc1)N(Cc1ccccc1)Cc1ccccc1`

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.

PA4446

Target candidate with partial support; inspect missing evidence before prioritizing.

Strengths

Risks / watch

Missing evidence

Overview

Target profile

Selected pocket evidence

Sequence

Functional Annotations

Gene Ontology (GO)

Sequence Features

3D Structure

Structural evidence

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Ligand evidence