Protein target profile

PA3717

FkbP-type peptidyl-prolyl cis-trans isomerase

Genome: NC_002516.2

Gene: PA3717 3D evidence: AlphaFold DB model UniProt Q9HXS4

Export view

Length 113

Pocket druggability 0.713

Ligand records 61

EC / GO 1 / 3

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: PA3717
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3717
Status: annotated
Amino acids: 113
3D evidence: AlphaFold DB model

5.2.1.8

GO:0003755 Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). GO:0000413 The modification of a protein by cis-trans isomerization of a proline residue. GO:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.

Target profile

Computed evidence for target prioritization.

Human off-target: Hit
Human identity (%): 58.182
Human E-value: 1.4e-14
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 0.713

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MNDRLQIEDLLLGDGKEVVKGALITTQYKGTLEDGTLFDSSYERGRPFQCVIGTGRVIKGWDQGLMGMKVGGKRRLFVPSHLAYGERQVGAHIKPHSNLLFEIELLEVLTRDD

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

5.2.1.8

Gene Ontology (GO)

GO:0003755 Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
GO:0000413 The modification of a protein by cis-trans isomerization of a proline residue.
GO:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.

Sequence Features

Domain/signature hits from InterPro and related databases.

10 records

Show feature table

Start	End	DB	Term	Name
17	109	PANTHER	PTHR45779	PEPTIDYLPROLYL ISOMERASE
17	109	InterPro	IPR044609	Peptidyl-prolyl cis-trans isomerase FKBP2/11
2	108	SUPERFAMILY	SSF54534	FKBP-like
17	106	Pfam	PF00254	FKBP-type peptidyl-prolyl cis-trans isomerase
17	106	InterPro	IPR001179	FKBP-type peptidyl-prolyl cis-trans isomerase domain
21	109	ProSiteProfiles	PS50059	FKBP-type peptidyl-prolyl cis-trans isomerase domain profile.
21	109	InterPro	IPR001179	FKBP-type peptidyl-prolyl cis-trans isomerase domain
1	112	Gene3D	G3DSA:3.10.50.40	-
1	112	InterPro	IPR046357	Peptidyl-prolyl cis-trans isomerase domain superfamily
1	110	FunFam	G3DSA:3.10.50.40:FF:000006	Peptidyl-prolyl cis-trans isomerase

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...

Legend High Medium Low

Structural evidence

0 + 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
AlphaFold DB PA3717	AlphaFold DB	—	—	full sequence	—	Viewing

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 #2

0.713

Show in viewer

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.

61 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 61 via homologs

Structural ligands 11 0 loaded crystals

Bioactive compounds 0 50 ZINC proposed compounds

Drug-like & clean 57 0 PAINS alerts

Best available ligand signal

4GI PDB via homolog 433.5 Da · LogP 2.71 · TPSA 119.7 Open detail RCSB PDB

Detail RCSB PDB 4GI PDB via homolog

Detail RCSB PDB 6UO PDB via homolog

Detail RCSB PDB 854 PDB via homolog

Detail RCSB PDB 861 PDB via homolog

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
4GI RCSB PDB	4GIV	Q3JK38	433.5 Da LogP 2.71 TPSA 119.7	✓ Ro5	✓ Clean	`c1cc(cc(c1)S(=O)(=O)N2CCCC[C@H]2C(=O)OCCCc3cccn…`
6UO RCSB PDB	5KLX	Q3JK38	432.5 Da LogP 2.17 TPSA 102.9	✓ Ro5	✓ Clean	`c1ccc(cc1)CS(=O)(=O)N2CCCC[C@H]2C(=O)OCCOC(=O)c…`
854 RCSB PDB	4FN2	Q3JK38	311.4 Da LogP 1.93 TPSA 63.7	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H]1CCCCN1S(=O)(=O)Cc2ccccc2`
861 RCSB PDB	4G50	Q3JK38	491.6 Da LogP 3.57 TPSA 91.4	✓ Ro5	✓ Clean	`COc1cc(cc(c1OC)OC)CCCOC(=O)[C@@H]2CCCCN2S(=O)(=…`
8ZV RCSB PDB	5V8T	Q63J95	578.7 Da LogP 2.39 TPSA 129.7	1 viol.	✓ Clean	`COCCOc1cc(cc(c1)OCCOC)C(=O)NCCOC(=O)[C@@H]2CCCC…`
FK5 RCSB PDB	1YAT	P20081	804.0 Da LogP 4.64 TPSA 178.4	2 viol.	✓ Clean	`C[C@@H]1C[C@@H]([C@@H]2[C@H](C[C@H]([C@@](O2)(C…`
JZF RCSB PDB	2KO7	Q63J95	367.4 Da LogP 1.32 TPSA 101.0	✓ Ro5	✓ Clean	`CCOC(=O)CN1C(=O)CC(CC1=O)C[C@H]([C@@H]2C[C@H](C…`
L2S RCSB PDB	2L2S	Q3JK38	249.4 Da LogP 3.10 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(cc1)SCC(=O)N2CCCCC2`
LL7 RCSB PDB	6O49	Q3JK38	519.6 Da LogP 2.54 TPSA 123.3	1 viol.	✓ Clean	`COc1cc(cc(c1OC)OC)NC(=O)CCNC(=O)[C@@H]2CCCCN2S(…`
LLD RCSB PDB	6O4A	Q3JK38	431.5 Da LogP 1.74 TPSA 105.7	✓ Ro5	✓ Clean	`c1ccc(cc1)CS(=O)(=O)N2CCCC[C@H]2C(=O)OCCNC(=O)c…`
R27 RCSB PDB	6VCT	U3N5X4	860.1 Da LogP 4.56 TPSA 202.7	2 viol.	✓ Clean	`C[C@@H]1C[C@@H]([C@@H]2[C@H](C[C@H]([C@@](O2)(C…`

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
ZINC449964 ZINC	1.000	249.4 Da LogP 3.10 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCCCC2)cc1`
ZINC454313 ZINC	1.000	263.4 Da LogP 3.49 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCCCCC2)cc1`
ZINC444277 ZINC	0.967	235.4 Da LogP 2.71 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCCC2)cc1`
ZINC12866189 ZINC	0.903	221.3 Da LogP 2.32 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCC2)cc1`
ZINC1133004 ZINC	0.839	414.6 Da LogP 3.86 TPSA 40.6	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCN(C(=O)CSc3ccc(C)cc3)CC2)cc1`
ZINC382512 ZINC	0.750	263.4 Da LogP 3.49 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCCC(=O)N2CCCCC2)cc1`
ZINC19792377 ZINC	0.743	264.4 Da LogP 1.86 TPSA 23.6	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCN(C)CC2)cc1`
ZINC89548993 ZINC	0.743	308.4 Da LogP 0.75 TPSA 60.9	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCN(C(=O)CO)CC2)cc1`
ZINC38079080 ZINC	0.735	279.4 Da LogP 3.28 TPSA 40.5	✓ Ro5	✓ Clean	`O=C(CSc1ccc(O)cc1)N1CCCCCCC1`
ZINC69846012 ZINC	0.725	346.5 Da LogP 2.95 TPSA 40.6	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCC[C@H](C(=O)N3CCCC3)C2)cc1`
ZINC69846019 ZINC	0.725	346.5 Da LogP 2.95 TPSA 40.6	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCC[C@@H](C(=O)N3CCCC3)C2)cc1`
ZINC444149 ZINC	0.722	251.4 Da LogP 1.95 TPSA 29.5	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCOCC2)cc1`
ZINC469815 ZINC	0.722	249.4 Da LogP 3.10 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCCC(=O)N2CCCC2)cc1`
ZINC3237508 ZINC	0.714	328.3 Da LogP 3.94 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(Br)cc1)N1CCCCCC1`
ZINC40159903 ZINC	0.714	253.3 Da LogP 2.93 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(F)cc1)N1CCCCC1`
ZINC443514 ZINC	0.714	269.8 Da LogP 3.44 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(Cl)cc1)N1CCCCC1`
ZINC452738 ZINC	0.714	283.8 Da LogP 3.83 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(Cl)cc1)N1CCCCCC1`
ZINC479739 ZINC	0.714	314.2 Da LogP 3.55 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(Br)cc1)N1CCCCC1`
ZINC2064548 ZINC	0.706	249.4 Da LogP 3.18 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccccc1)N1CCCCCC1`
ZINC38078738 ZINC	0.706	237.3 Da LogP 2.11 TPSA 40.5	✓ Ro5	✓ Clean	`O=C(CSc1ccc(O)cc1)N1CCCC1`
ZINC443732 ZINC	0.706	235.4 Da LogP 2.79 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccccc1)N1CCCCC1`
ZINC6742623 ZINC	0.706	263.4 Da LogP 3.57 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccccc1)N1CCCCCCC1`
ZINC19849974 ZINC	0.703	278.4 Da LogP 2.25 TPSA 23.6	✓ Ro5	✓ Clean	`CCN1CCN(C(=O)CSc2ccc(C)cc2)CC1`
ZINC20451735 ZINC	0.703	265.4 Da LogP 2.80 TPSA 29.5	✓ Ro5	✓ Clean	`COc1ccc(SCC(=O)N2CCCCC2)cc1`
ZINC309273 ZINC	0.703	263.4 Da LogP 3.35 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCC(C)CC2)cc1`
ZINC40047465 ZINC	0.692	292.4 Da LogP 1.83 TPSA 49.4	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)NCC(=O)N2CCCC2)cc1`
ZINC459910 ZINC	0.692	292.4 Da LogP 1.81 TPSA 63.4	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCC(C(N)=O)CC2)cc1`
ZINC22220121 ZINC	0.686	265.3 Da LogP 2.10 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(SCC(=O)N2CCCC2)cc1`
ZINC2845544 ZINC	0.686	239.3 Da LogP 2.54 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(F)cc1)N1CCCC1`
ZINC3233408 ZINC	0.686	300.2 Da LogP 3.16 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(Br)cc1)N1CCCC1`
ZINC443844 ZINC	0.686	255.8 Da LogP 3.05 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(Cl)cc1)N1CCCC1`
ZINC616584 ZINC	0.684	322.4 Da LogP 2.39 TPSA 49.9	✓ Ro5	✓ Clean	`CCOC(=O)N1CCN(C(=O)CSc2ccc(C)cc2)CC1`
ZINC9591604 ZINC	0.684	292.4 Da LogP 2.75 TPSA 49.4	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(SCC(=O)N2CCCCC2)cc1`
ZINC561733 ZINC	0.676	221.3 Da LogP 2.40 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccccc1)N1CCCC1`
ZINC12977119 ZINC	0.676	249.4 Da LogP 3.02 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCCC2)cc1C`
ZINC20484525 ZINC	0.676	251.4 Da LogP 2.41 TPSA 29.5	✓ Ro5	✓ Clean	`COc1ccc(SCC(=O)N2CCCC2)cc1`
ZINC621674 ZINC	0.659	321.4 Da LogP 2.89 TPSA 46.6	✓ Ro5	✓ Clean	`CCOC(=O)[C@H]1CCCN(C(=O)CSc2ccc(C)cc2)C1`
ZINC621675 ZINC	0.659	321.4 Da LogP 2.89 TPSA 46.6	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H]1CCCN(C(=O)CSc2ccc(C)cc2)C1`
ZINC18044105 ZINC	0.658	277.4 Da LogP 3.59 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2C[C@@H](C)C[C@@H](C)C2)cc1`
ZINC620052 ZINC	0.658	277.4 Da LogP 3.59 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2C[C@@H](C)C[C@H](C)C2)cc1`
ZINC620053 ZINC	0.658	277.4 Da LogP 3.59 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2C[C@H](C)C[C@@H](C)C2)cc1`
ZINC8393831 ZINC	0.658	278.4 Da LogP 2.36 TPSA 49.4	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(SCC(=O)N2CCCC2)cc1`
ZINC328890 ZINC	0.650	326.5 Da LogP 3.44 TPSA 23.6	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCN(c3ccccc3)CC2)cc1`
ZINC40025614 ZINC	0.650	350.5 Da LogP 3.17 TPSA 49.9	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCN(C(=O)OC(C)(C)C)CC2)cc1`
ZINC459923 ZINC	0.643	321.4 Da LogP 2.89 TPSA 46.6	✓ Ro5	✓ Clean	`CCOC(=O)C1CCN(C(=O)CSc2ccc(C)cc2)CC1`
ZINC2625205 ZINC	0.641	263.4 Da LogP 3.41 TPSA 20.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCCCC2)c(C)c1`
ZINC12913966 ZINC	0.639	241.7 Da LogP 2.66 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(Cl)cc1)N1CCC1`
ZINC12973358 ZINC	0.639	225.3 Da LogP 2.15 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(F)cc1)N1CCC1`
ZINC12973852 ZINC	0.639	286.2 Da LogP 2.77 TPSA 20.3	✓ Ro5	✓ Clean	`O=C(CSc1ccc(Br)cc1)N1CCC1`
ZINC69348894 ZINC	0.636	342.5 Da LogP 2.62 TPSA 49.3	✓ Ro5	✓ Clean	`Cc1ccc(SCC(=O)N2CCCN(c3ncccn3)CC2)cc1`

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.