Protein profile

VK055_1436

putA bifunctional enzyme and transcriptional regulator PutA transcriptional repressor, Proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase

Genome: KpATCC43816

Gene: AIK80057.1 Structure source: ColabFold UniProt A0A9Q9Q9F8

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Amino acids 1320

Annotations 13

Features 42

PDB binders 17

Druggability 0.964

Overview

Basic information about this protein and its source genome.

Accession: VK055_1436
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: AIK80057.1
Status: annotated
Amino acids: 1320
Structure source: ColabFold

GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0010133 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-proline into L-glutamate. GO:0006561 OBSOLETE. The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins. GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. GO:0003842 L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + 2 H+.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 34.653
Human E-value: 2.37e-25
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 37.336
Localization: Cytoplasmic
ColabFold pLDDT: 90.52

Selected Druggability evidence

ColabFold / curated model

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 0.964

Structure CB_VK055_1436

Pocket Pocket 21

P2Rank 0.98

Structure CB_VK055_1436

Pocket Pocket 1

ColabFold model

FPocket 0.964 · Pocket 21

P2Rank 0.98 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 147 / 4744 genomes with a hit

Normalized 0.031

Sequence

Primary amino-acid sequence viewer.

MGTTTMGVKLDDATRERIKSAASRIDRTPHWLIKQAIFNYLEKLENDETLPELPALLSGAANESDDASVPTEEPYQPFLEFAEQILPQSVSRAAITAAWRRPETDAVPMLLEQARLPQPLGEQAHKLAYQLAEKLRNQKTASGRAGMVQSLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNETSLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMEGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADNTLPLDELVADPVSAVEKLAQQEGQAGLPHPKIPLPRDLYGSGRSNSAGLDLANEHRLASLSSSLLNSALHKWQALPMLEQPVAEGEMQPVVNPAEPKDIVGYVREASDAEVQQALTSAINNAPIWFATPPQERAAILERAAVLMESQMPTLMGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTSDERVRGVMFTGSTEVATLLQRNIASRLDPQGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQEEVADHTLTMLRGAMSECRMGNPGRLTTDIGPVIDAEAKENIERHIQAMRAKGRTVYQAVRENSEDAREWRHGTFVPPTLIELDSFDELKKEVFGPVLHVVRYNRNELDKLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSRPQDAVGVTFARQDAERPLDAQLKTLLEKPLQALQQWAAGRPELQALCQQYSEQAQSGTQRLLPGPTGERNTLTLMPRERVLCVADNEQDALIQLAAVLAVGCEVLWPDSALQRDLAKKLPREVSERIRFAKAEQLPGQAFDAVIYHGDSDQLRELCEQVAARDGAIVSVQGFARGETNLLLERLYIERSLSVNTAAAGGNASLMTIG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

13 GO

Gene Ontology (GO)

GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0010133 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-proline into L-glutamate.
GO:0006561 OBSOLETE. The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
GO:0003842 L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + 2 H+.
GO:0003700 A transcription regulator activity that modulates transcription of gene sets via selective and non-covalent binding to a specific double-stranded genomic DNA sequence (sometimes referred to as a motif) within a cis-regulatory region. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units, and include bacterial operons.
GO:0004657 Catalysis of the reaction: L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol + H+.
GO:0009898 The leaflet of the plasma membrane that faces the cytoplasm, including any protein embedded in, attached to, or peripherally associated with it.
GO:0043168 Binding to an anion, a charged atom or group of atoms with a net negative charge.
GO:0001217 A DNA-binding transcription factor activity that represses or decreases the transcription of specific gene sets.
GO:1901363 Binding to heterocyclic compound.
GO:0000976 Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.

Sequence Features

Domain/signature hits from InterPro and related databases.

42 records

Show feature table

Start	End	DB	Term	Name
148	259	Pfam	PF14850	DNA-binding domain of Proline dehydrogenase
148	259	InterPro	IPR024082	Proline dehydrogenase PutA, domain II
218	610	FunFam	G3DSA:3.20.20.220:FF:000004	Bifunctional protein PutA
652	891	FunFam	G3DSA:3.40.605.10:FF:000017	Bifunctional protein PutA
3	45	SUPERFAMILY	SSF47598	Ribbon-helix-helix
3	45	InterPro	IPR010985	Ribbon-helix-helix
910	921	ProSitePatterns	PS00070	Aldehyde dehydrogenases cysteine active site.
910	921	InterPro	IPR016160	Aldehyde dehydrogenase, cysteine active site
162	187	FunFam	G3DSA:1.20.5.460:FF:000001	Bifunctional protein PutA
656	1112	SUPERFAMILY	SSF53720	ALDH-like
656	1112	InterPro	IPR016161	Aldehyde/histidinol dehydrogenase
87	138	Gene3D	G3DSA:1.20.5.550	Single Helix bin
87	138	InterPro	IPR024090	Proline dehydrogenase PutA, domain I
659	1106	Pfam	PF00171	Aldehyde dehydrogenase family
659	1106	InterPro	IPR015590	Aldehyde dehydrogenase domain
885	1082	FunFam	G3DSA:3.40.309.10:FF:000005	1-pyrroline-5-carboxylate dehydrogenase 1
237	1318	PANTHER	PTHR42862	DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED
88	261	SUPERFAMILY	SSF81935	N-terminal domain of bifunctional PutA protein
88	261	InterPro	IPR024089	Proline dehydrogenase PutA, domain I/II
885	1082	Gene3D	G3DSA:3.40.309.10	Aldehyde Dehydrogenase; Chain A, domain 2
885	1082	InterPro	IPR016163	Aldehyde dehydrogenase, C-terminal
219	610	Gene3D	G3DSA:3.20.20.220	-
262	618	SUPERFAMILY	SSF51730	FAD-linked oxidoreductase
262	618	InterPro	IPR029041	FAD-linked oxidoreductase-like
653	1113	Gene3D	G3DSA:3.40.605.10	Aldehyde Dehydrogenase; Chain A, domain 1
653	1113	InterPro	IPR016162	Aldehyde dehydrogenase, N-terminal
269	569	Pfam	PF01619	Proline dehydrogenase
269	569	InterPro	IPR002872	Proline dehydrogenase domain
610	1113	NCBIfam	TIGR01238	L-glutamate gamma-semialdehyde dehydrogenase
610	1113	InterPro	IPR005933	Bifunctional protein PutA, C-terminal domain
643	1119	CDD	cd07125	ALDH_PutA-P5CDH
74	1320	PIRSF	PIRSF000197	Bifunct_PutA
74	1320	InterPro	IPR025703	Bifunctional protein PutA
162	187	Gene3D	G3DSA:1.20.5.460	Single helix bin
11	52	Gene3D	G3DSA:1.10.1220.10	-
11	52	InterPro	IPR013321	Arc-type ribbon-helix-helix
4	46	CDD	cd22233	RHH_CopAso-like
89	136	Pfam	PF18327	Proline utilization A proline dehydrogenase N-terminal domain
89	136	InterPro	IPR041349	Proline utilization A proline dehydrogenase N-terminal domain
882	889	ProSitePatterns	PS00687	Aldehyde dehydrogenases glutamic acid active site.
882	889	InterPro	IPR029510	Aldehyde dehydrogenase, glutamic acid active site
87	138	FunFam	G3DSA:1.20.5.550:FF:000001	Bifunctional protein PutA

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
ColabFold VK055_1436	ColabFold	—	—	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
21				0.964
2				0.409
56				0.302

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	29.14	0.929
2	20.9	0.863
3	20.46	0.855
4	7.0	0.362
5	5.81	0.284

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.

67 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
2L3	4NMF	Q746X3	254.3 Da LogP 1.10 TPSA 88.5	✓ Ro5	Alert	`C[C@]1(CC(=O)c2ccccc2C1=O)S(=O)(=O)O`
2OP	1TJ0	P09546	90.1 Da LogP -0.55 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)O`
C15	4NMC	Q746X3	336.6 Da LogP 4.26 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
DPR	2EJ6	Q5SI02	115.1 Da LogP -0.18 TPSA 49.3	✓ Ro5	✓ Clean	`C1C[C@@H](NC1)C(=O)O`
FDA	3ITG	P09546	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
HYP	3E2Q	P09546	131.1 Da LogP -1.21 TPSA 69.6	✓ Ro5	✓ Clean	`C1[C@H](CN[C@@H]1C(=O)O)O`
P5F	5UR2	Q6MNK1	—	—	—	`CC1=CC2=[N](C3=C(C(=O)NC(=O)N3)[N](=C2C=C1C)C=C…`
SO2	2FZM	P09546	64.1 Da LogP -0.67 TPSA 34.1	✓ Ro5	✓ Clean	`O=S=O`
TFB	1TIW	P09546	116.1 Da LogP 0.25 TPSA 46.5	✓ Ro5	✓ Clean	`C1C[C@H](OC1)C(=O)O`
UJD	7MY9	F7X6I3	150.2 Da LogP 0.88 TPSA 37.3	✓ Ro5	✓ Clean	`C1CSC(S1)C(=O)O`
UJM	7MYB	F7X6I3	132.2 Da LogP 0.97 TPSA 37.3	✓ Ro5	✓ Clean	`C1C[C@H](SC1)C(=O)O`
UJP	7MYB	F7X6I3	132.2 Da LogP 0.97 TPSA 37.3	✓ Ro5	✓ Clean	`C1C[C@@H](SC1)C(=O)O`
UY7	6X9A	F7X6I3	131.1 Da LogP -1.21 TPSA 69.6	✓ Ro5	✓ Clean	`C1[C@@H](CN[C@H]1C(=O)O)O`
UYA	6X9B	F7X6I3	131.1 Da LogP -1.21 TPSA 69.6	✓ Ro5	✓ Clean	`C1[C@H](CN[C@H]1C(=O)O)O`
ZPJ	7MWV	P09546	86.1 Da LogP 0.48 TPSA 37.3	✓ Ro5	✓ Clean	`C1CC1C(=O)O`
ZPM	7MWU	P09546	100.1 Da LogP 0.87 TPSA 37.3	✓ Ro5	✓ Clean	`C1CC(C1)C(=O)O`
ZPS	7MWT	P09546	144.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C1CC(C1)(C(=O)O)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
ZINC14880434	1.000	336.6 Da LogP 4.26 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC1999508	1.000	254.3 Da LogP 1.10 TPSA 88.5	✓ Ro5	Alert	`C[C@@]1(S(=O)(=O)O)CC(=O)c2ccccc2C1=O`
ZINC1999509	1.000	254.3 Da LogP 1.10 TPSA 88.5	✓ Ro5	Alert	`C[C@]1(S(=O)(=O)O)CC(=O)c2ccccc2C1=O`
ZINC2384686	1.000	280.5 Da LogP 2.70 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC5029952	1.000	200.2 Da LogP 1.74 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C1CCCC(C(=O)O)CCC1`
ZINC58541260	1.000	308.5 Da LogP 3.48 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC4521338	0.813	212.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)C1CCCCCCCCCCC1`
ZINC2325704365	0.800	254.3 Da LogP 2.77 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CC[C@H]([C@H]2CC[C@H](C(=O)O)CC2)CC1`
ZINC1532902	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC2379127	0.655	212.3 Da LogP -0.67 TPSA 74.6	✓ Ro5	✓ Clean	`C[N+](C)(CCO)CCCS(=O)(=O)O`
ZINC100019805	0.654	292.5 Da LogP 4.97 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCS(=O)(=O)O`
ZINC1625794	0.654	264.4 Da LogP 4.19 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCS(=O)(=O)O`
ZINC1651926	0.654	250.4 Da LogP 3.80 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCS(=O)(=O)O`
ZINC1843748	0.654	222.3 Da LogP 3.01 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCS(=O)(=O)O`
ZINC2515939	0.654	236.4 Da LogP 3.41 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCS(=O)(=O)O`
ZINC42921009	0.654	278.5 Da LogP 4.58 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCS(=O)(=O)O`
ZINC80135680	0.654	208.3 Da LogP 2.62 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCS(=O)(=O)O`
ZINC3593496	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC101661450	0.649	407.6 Da LogP 3.77 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)NCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC97943292	0.649	435.7 Da LogP 4.55 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)NCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC14686440	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC117798402	0.611	216.2 Da LogP 0.27 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CC[C@@H](C(=O)O)[C@@H](C(=O)O)C1`
ZINC44069472	0.611	216.2 Da LogP 0.27 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CC[C@@H](C(=O)O)C[C@H]1C(=O)O`
ZINC60121565	0.611	240.3 Da LogP 2.52 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C1CCC2(CC1)CCC(C(=O)O)CC2`
ZINC153514	0.609	211.3 Da LogP 1.11 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)C1CCN(C(=O)C2CCC2)CC1`
ZINC757066037	0.609	200.2 Da LogP 1.44 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CCC[C@@H](C(=O)O)CC1`
ZINC757066044	0.609	200.2 Da LogP 1.44 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@@H]1CCC[C@H](C(=O)O)CC1`
ZINC757066048	0.609	200.2 Da LogP 1.44 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CCC[C@@H](C(=O)O)CC1`
ZINC757066049	0.609	200.2 Da LogP 1.44 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)[C@H]1CCC[C@H](C(=O)O)CC1`
ZINC103598261	0.600	297.4 Da LogP 2.36 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CC[C@@H](CNC[C@H]2CC[C@@H](C(=O)O)C…`
ZINC14806503	0.600	216.2 Da LogP 0.27 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)C1CC(C(=O)O)CC(C(=O)O)C1`
ZINC245204662	0.600	216.2 Da LogP 0.27 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)[C@H]1C[C@@H](C(=O)O)C[C@@H](C(=O)O)C1`
ZINC100050172	0.588	352.6 Da LogP 3.23 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)C[C@H](O)CS(=O)(=O)O`
ZINC100050174	0.588	352.6 Da LogP 3.23 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)C[C@@H](O)CS(=O)(=O)O`
ZINC13398039	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC108246896	0.571	206.3 Da LogP 0.67 TPSA 71.4	✓ Ro5	✓ Clean	`CS(=O)(=O)C1CCC(C(=O)O)CC1`
ZINC261596316	0.571	225.3 Da LogP 1.50 TPSA 57.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CC[C@H](C(=O)N2CCCC2)CC1`
ZINC307226840	0.571	207.3 Da LogP -0.08 TPSA 97.5	✓ Ro5	✓ Clean	`NS(=O)(=O)C1CCC(C(=O)O)CC1`
ZINC31729329	0.571	240.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)C1(C(=O)O)CCC2(CCCCC2)CC1`
ZINC37472008	0.571	211.3 Da LogP 1.16 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)C1CCC(NC(=O)C2CC2)CC1`
ZINC6741121	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@@H]1CCCO1)N1CCCCCCC1`
ZINC6741122	0.571	211.3 Da LogP 1.96 TPSA 29.5	✓ Ro5	✓ Clean	`O=C([C@H]1CCCO1)N1CCCCCCC1`
ZINC108323602	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(O)[C@H]1CCCCC[C@H]1NC(=O)[C@H]1CCCO1`
ZINC157702634	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(N[C@@H]1CCCCC[C@H]1C(=O)O)[C@H]1CCCO1`
ZINC94744170	0.563	255.3 Da LogP 1.32 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(N[C@@H]1CCCCC[C@@H]1C(=O)O)[C@@H]1CCCO1`

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.