KpATCC43816 Protein target profile

peptidyl-prolyl cis-trans isomerase

Accession: VK055_2524

Gene: AIK81121.1 surA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GI34

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Length 428

Pocket druggability (P2Rank · AlphaFold DB model) 0.769

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 7 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.77. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

Terms and data sources used on 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 Target 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.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: No hit
Gut microbiome similarity: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 90.888 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 89.32 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.769

Structure A0A0H3GI34

Pocket Pocket 1

Druggability (FPocket) 0.5

Structure A0A0H3GI34

Pocket Pocket 21

ColabFold model

P2Rank 0.709 · Pocket 1

FPocket 0.507 · Pocket 25

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 110 / 4744 genomes with a hit

Prevalence 2.3%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: no human homolog detected.

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKNWKTLLLGIAMIANTSFAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAGQAGQQLPDDATLRHQILERLIMDQIVLQMGQKMGVKISDDQLDQAIANIAKQNNMTLDQMRSRLAYEGINYNTYRNQIRKEMLISEVRNNEVRRRITVLPQEVEALAKQIGDQNDASTELNLSHILIPLPENPTSDEVAAAQEQANSIVEQARNGANFGKLAITYSADQQALKGGQMGWGRIQELPGIFAQALSTAKKGDIVGPIRSGVGFHILKVNDLRGGTQNISVTEVHARHILLKPSPIMNDAQAQAKLEQIAAEIKSGKITFAQAAKTYSEDPGSANQGGDLGWATPDIFDPAFRDALMRLNKGQTSGPVHSSFGWHLIELLDSRQVDRTDAAQKDRAYRMLMNRKFSEEAATWMQEQRASAYVKILSN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: Periplasmic

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:0050821 Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
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:0051082 Binding to an unfolded protein.
GO:0042277 Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds.
GO:0043165 The assembly of an outer membrane of the type formed in Gram-negative bacteria. This membrane is enriched in polysaccharide and protein, and the outer leaflet of the membrane contains specific lipopolysaccharide structures.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
21	428	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
25	142	Pfam	PF09312	SurA N-terminal domain
25	142	InterPro	IPR015391	SurA N-terminal
283	384	SUPERFAMILY	SSF54534	FKBP-like
382	428	Gene3D	G3DSA:1.10.4030.10	-
21	148	FunFam	G3DSA:1.10.4030.10:FF:000002	Chaperone SurA
1	20	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
280	381	FunFam	G3DSA:3.10.50.40:FF:000007	Chaperone SurA
280	381	Gene3D	G3DSA:3.10.50.40	-
280	381	InterPro	IPR046357	Peptidyl-prolyl cis-trans isomerase domain superfamily
25	201	SUPERFAMILY	SSF109998	Triger factor/SurA peptide-binding domain-like
25	201	InterPro	IPR027304	Trigger factor/SurA domain superfamily
178	272	Pfam	PF00639	PPIC-type PPIASE domain
178	272	InterPro	IPR000297	Peptidyl-prolyl cis-trans isomerase, PpiC-type
173	275	SUPERFAMILY	SSF54534	FKBP-like
282	382	ProSiteProfiles	PS50198	PpiC-type peptidyl-prolyl cis-trans isomerase family profile.
282	382	InterPro	IPR000297	Peptidyl-prolyl cis-trans isomerase, PpiC-type
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
7	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
16	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
321	342	ProSitePatterns	PS01096	PpiC-type peptidyl-prolyl cis-trans isomerase signature.
321	342	InterPro	IPR023058	Peptidyl-prolyl cis-trans isomerase, PpiC-type, conserved site
21	148	Gene3D	G3DSA:1.10.4030.10	-
1	277	PANTHER	PTHR47637	CHAPERONE SURA
171	272	ProSiteProfiles	PS50198	PpiC-type peptidyl-prolyl cis-trans isomerase family profile.
171	272	InterPro	IPR000297	Peptidyl-prolyl cis-trans isomerase, PpiC-type
1	20	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
283	383	Pfam	PF13616	PPIC-type PPIASE domain
163	279	Gene3D	G3DSA:3.10.50.40	-
163	279	InterPro	IPR046357	Peptidyl-prolyl cis-trans isomerase domain superfamily
1	6	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
9	428	Hamap	MF_01183	Chaperone SurA [surA].
9	428	InterPro	IPR023034	Peptidyl-prolyl isomerase SurA

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.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

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

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.769

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Surrounding area

Pocket 2 P2Rank #2

0.355

Likely same site as FPocket 15 0.8 Å 10 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.071

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Surrounding area

Pocket 4 P2Rank #4

0.041

Likely same site as FPocket 21 2.1 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.035

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #21

0.5 Unusual size

Likely same site as P2Rank 4 2.1 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #15

0.35

Likely same site as P2Rank 2 0.8 Å 10 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.709

Likely same site as FPocket 25 4.1 Å 14 shared residues 93% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.448

Likely same site as FPocket 8 0.9 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.185

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Surrounding area

Pocket 4 P2Rank #4

0.098

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Surrounding area

Pocket 5 P2Rank #5

0.075

Likely same site as FPocket 5 2.9 Å 9 shared residues 75% of smaller site

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #25

0.507

Likely same site as P2Rank 1 4.1 Å 14 shared residues 93% of smaller site

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Surrounding area

Pocket 2 FPocket #8

0.395

Likely same site as P2Rank 2 0.9 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #5

0.306

Likely same site as P2Rank 5 2.9 Å 9 shared residues 75% of smaller site

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Surrounding area

Pocket 4 FPocket #24

0.247

Likely same site as P2Rank 5 4.3 Å 8 shared residues 67% of smaller site

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

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 AF_A0A0H3GI34	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2524	ColabFold	—	—	full sequence	—	Loaded

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 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2NV PDB via homolog 279.4 Da · LogP 0.44 · TPSA 72.2 Open detail RCSB PDB

D1D PDB via homolog Detail RCSB PDB

ICB PDB via homolog Detail RCSB PDB

ZINC142395 ZINC proposed compound · Tanimoto 0.700 Detail ZINC

ZINC141246167 ZINC proposed compound · Tanimoto 0.667 Detail ZINC

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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
2NV RCSB PDB	6VJ6	Q81CB1	279.4 Da LogP 0.44 TPSA 72.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOC[C@@H](C)N`
D1D RCSB PDB	3UI5	Q9Y237	152.2 Da LogP 0.10 TPSA 40.5	✓ Ro5	✓ Clean	`C1[C@H]([C@@H](CSS1)O)O`
ICB RCSB PDB	5EZ1	P56112	161.2 Da LogP 1.87 TPSA 53.1	✓ Ro5	✓ Clean	`c1ccc2c(c1)cc([nH]2)C(=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
ZINC142395 ZINC	0.700	221.3 Da LogP 3.40 TPSA 32.9	✓ Ro5	✓ Clean	`O=C(c1ccccc1)c1cc2ccccc2[nH]1`
ZINC141246167 ZINC	0.667	319.3 Da LogP 3.60 TPSA 98.0	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(NC(=O)c3cc4ccccc4[nH]3)ccc2[nH]1`
ZINC2384034 ZINC	0.667	205.2 Da LogP 1.56 TPSA 90.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc2cc(C(=O)O)[nH]c2c1`
ZINC11866572 ZINC	0.656	372.4 Da LogP 3.25 TPSA 72.2	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)N1CCN(C(=O)c2cc3ccccc3[nH]…`
ZINC32003100 ZINC	0.656	237.3 Da LogP 3.53 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(-c3ccccc3)ccc2[nH]1`
ZINC3748671 ZINC	0.656	237.3 Da LogP 3.53 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2ccc(-c3ccccc3)cc2[nH]1`
ZINC74002845 ZINC	0.656	226.2 Da LogP 2.86 TPSA 68.9	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2cc3ccccc3[nH]2)[nH]1`
ZINC384465 ZINC	0.636	236.3 Da LogP 3.42 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1)c1cc2ccccc2[nH]1`
ZINC12919870 ZINC	0.618	214.3 Da LogP 2.40 TPSA 36.1	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)N1CCCC1`
ZINC2582702 ZINC	0.613	205.2 Da LogP 1.56 TPSA 90.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc2[nH]c(C(=O)O)cc2c1`
ZINC2582710 ZINC	0.613	240.1 Da LogP 2.63 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2ccc(Br)cc2[nH]1`
ZINC402742 ZINC	0.613	240.1 Da LogP 2.63 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(Br)ccc2[nH]1`
ZINC20728176 ZINC	0.611	301.3 Da LogP 0.54 TPSA 93.7	✓ Ro5	✓ Clean	`O=C(O)C(=O)N1CCN(C(=O)c2cc3ccccc3[nH]2)CC1`
ZINC23788096 ZINC	0.611	333.4 Da LogP 2.77 TPSA 56.4	✓ Ro5	✓ Clean	`O=C(c1ccccc1)N1CCN(C(=O)c2cc3ccccc3[nH]2)CC1`
ZINC23582 ZINC	0.606	211.2 Da LogP 3.02 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2c(ccc3ccccc32)[nH]1`
ZINC39341723 ZINC	0.606	203.2 Da LogP 2.07 TPSA 70.2	✓ Ro5	✓ Clean	`CC(=O)c1ccc2cc(C(=O)O)[nH]c2c1`
ZINC19843563 ZINC	0.600	218.2 Da LogP 0.98 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)c1cc2ccccc2[nH]1`
ZINC263620956 ZINC	0.600	287.3 Da LogP 4.69 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2c(-c3cccc4ccccc34)cccc2[nH]1`
ZINC338381 ZINC	0.600	250.3 Da LogP 3.44 TPSA 36.1	✓ Ro5	✓ Clean	`CN(C(=O)c1cc2ccccc2[nH]1)c1ccccc1`
ZINC35133185 ZINC	0.600	256.3 Da LogP 3.57 TPSA 36.1	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)N1CCCCCCC1`
ZINC6344517 ZINC	0.600	253.3 Da LogP 3.66 TPSA 62.3	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(Oc3ccccc3)ccc2[nH]1`
ZINC7911351 ZINC	0.600	228.3 Da LogP 2.79 TPSA 36.1	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)N1CCCCC1`
ZINC7912494 ZINC	0.600	242.3 Da LogP 3.18 TPSA 36.1	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)N1CCCCCC1`
ZINC2432858 ZINC	0.594	287.1 Da LogP 2.47 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2cc(I)ccc2[nH]1`
ZINC2443762 ZINC	0.594	287.1 Da LogP 2.47 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2ccc(I)cc2[nH]1`
ZINC12390058 ZINC	0.583	271.3 Da LogP 1.47 TPSA 56.4	✓ Ro5	✓ Clean	`CC(=O)N1CCN(C(=O)c2cc3ccccc3[nH]2)CC1`
ZINC16636620 ZINC	0.583	326.4 Da LogP 4.69 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(NC(c1ccccc1)c1ccccc1)c1cc2ccccc2[nH]1`
ZINC509902 ZINC	0.583	229.3 Da LogP 1.21 TPSA 48.1	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)N1CCNCC1`
ZINC5531695 ZINC	0.583	251.3 Da LogP 3.52 TPSA 42.1	✓ Ro5	✓ Clean	`O=C(OCc1ccccc1)c1cc2ccccc2[nH]1`
ZINC6649233 ZINC	0.583	250.3 Da LogP 3.10 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(NCc1ccccc1)c1cc2ccccc2[nH]1`
ZINC2512141 ZINC	0.579	305.4 Da LogP 3.13 TPSA 39.3	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)N1CCN(c2ccccc2)CC1`
ZINC3163645 ZINC	0.576	211.2 Da LogP 3.02 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)c1cc2ccc3ccccc3c2[nH]1`
ZINC12946715 ZINC	0.571	202.3 Da LogP 2.31 TPSA 44.9	✓ Ro5	✓ Clean	`CC(C)NC(=O)c1cc2ccccc2[nH]1`
ZINC9970537 ZINC	0.571	217.3 Da LogP 3.12 TPSA 42.1	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)c1cc2ccccc2[nH]1`
ZINC19843564 ZINC	0.568	232.2 Da LogP 1.37 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(O)CCNC(=O)c1cc2ccccc2[nH]1`
ZINC19843565 ZINC	0.568	232.2 Da LogP 1.37 TPSA 82.2	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)c1cc2ccccc2[nH]1)C(=O)O`
ZINC19868744 ZINC	0.568	243.3 Da LogP 1.56 TPSA 39.3	✓ Ro5	✓ Clean	`CN1CCN(C(=O)c2cc3ccccc3[nH]2)CC1`
ZINC23549857 ZINC	0.568	299.4 Da LogP 2.82 TPSA 67.0	✓ Ro5	✓ Clean	`O=C(CS(=O)(=O)c1ccccc1)c1cc2ccccc2[nH]1`
ZINC344370 ZINC	0.568	230.3 Da LogP 1.64 TPSA 45.3	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)N1CCOCC1`
ZINC36163408 ZINC	0.568	246.3 Da LogP 2.36 TPSA 36.1	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)N1CCSCC1`
ZINC9420925 ZINC	0.568	232.2 Da LogP 1.37 TPSA 82.2	✓ Ro5	✓ Clean	`C[C@H](NC(=O)c1cc2ccccc2[nH]1)C(=O)O`
ZINC14985707 ZINC	0.559	203.2 Da LogP 2.07 TPSA 70.2	✓ Ro5	✓ Clean	`CC(=O)c1ccc2[nH]c(C(=O)O)cc2c1`
ZINC2582700 ZINC	0.559	217.3 Da LogP 3.16 TPSA 53.1	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc2[nH]c(C(=O)O)cc2c1`
ZINC3748697 ZINC	0.559	217.3 Da LogP 3.16 TPSA 53.1	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc2cc(C(=O)O)[nH]c2c1`
ZINC13956836 ZINC	0.556	204.2 Da LogP 0.89 TPSA 65.1	✓ Ro5	✓ Clean	`O=C(NCCO)c1cc2ccccc2[nH]1`
ZINC14796789 ZINC	0.556	200.2 Da LogP 2.06 TPSA 44.9	✓ Ro5	✓ Clean	`O=C(NC1CC1)c1cc2ccccc2[nH]1`
ZINC15779808 ZINC	0.556	260.3 Da LogP 3.88 TPSA 48.6	✓ Ro5	✓ Clean	`O=C(c1cc2ccccc2[nH]1)c1c[nH]c2ccccc12`
ZINC261232647 ZINC	0.556	219.2 Da LogP 1.65 TPSA 79.4	✓ Ro5	✓ Clean	`COC(=O)c1ccc2cc(C(=O)O)[nH]c2c1`
ZINC38235439 ZINC	0.556	204.2 Da LogP 1.80 TPSA 45.3	✓ Ro5	✓ Clean	`CON(C)C(=O)c1cc2ccccc2[nH]1`
ZINC13681944 ZINC	0.553	294.3 Da LogP 2.72 TPSA 82.2	✓ Ro5	✓ Clean	`O=C(N[C@H](C(=O)O)c1ccccc1)c1cc2ccccc2[nH]1`

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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GI34

Pathways

BioCyc PEPTIDYLPROLYL-ISOMERASE-RXN[CCO-CYTOSOL]-CPD-8624//CPD-8625.32. BioCyc PEPTIDYLPROLYL-ISOMERASE-RXN[CCO-PERI-BAC]-CPD-8624//CPD-8625.33.