Protein profile

VK055_2450

dihydrolipoyl dehydrogenase

Genome: KpATCC43816

Gene: AIK81047.1 lpdA2 Structure source: AlphaFold + ColabFold UniProt A0A0H3GJD9

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Amino acids 474

Annotations 8

Features 38

PDB binders 14

Druggability 0.981

Overview

Basic information about this protein and its source genome.

Accession: VK055_2450
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: AIK81047.1 lpdA2
Status: annotated
Amino acids: 474
Structure source: AlphaFold + ColabFold

1.8.1.4

GO:0004148 Catalysis of the reaction: N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ = N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH + H+. GO:0016668 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing 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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0006103 The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 52.778
Human E-value: 7.09e-16
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 98.312
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 97.1

Selected Druggability evidence

AlphaFold / UniProt 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 0.981

Structure A0A0H3GJD9

Pocket Pocket 33

P2Rank 0.953

Structure A0A0H3GJD9

Pocket Pocket 1

ColabFold model

FPocket 0.923 · Pocket 28

P2Rank 0.982 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 172 / 4744 genomes with a hit

Normalized 0.036

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1.8.1.4

Gene Ontology (GO)

GO:0004148 Catalysis of the reaction: N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD+ = N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH + H+.
GO:0016668 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing 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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0006103 The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
347	455	Pfam	PF02852	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
347	455	InterPro	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
4	458	PANTHER	PTHR22912	DISULFIDE OXIDOREDUCTASE
346	467	Gene3D	G3DSA:3.30.390.30	-
346	467	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
7	460	NCBIfam	TIGR01350	dihydrolipoyl dehydrogenase
7	460	InterPro	IPR006258	Dihydrolipoamide dehydrogenase
343	466	SUPERFAMILY	SSF55424	FAD/NAD-linked reductases, dimerisation (C-terminal) domain
343	466	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
1	469	PIRSF	PIRSF000350	Hg-II_reductase_MerA
1	469	InterPro	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I
7	154	FunFam	G3DSA:3.50.50.60:FF:000001	Dihydrolipoyl dehydrogenase, mitochondrial
346	466	FunFam	G3DSA:3.30.390.30:FF:000001	Dihydrolipoyl dehydrogenase
150	271	Gene3D	G3DSA:3.50.50.60	-
150	271	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
408	423	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
141	150	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
430	450	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
177	202	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
343	364	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
41	56	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
265	279	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
308	315	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
8	30	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
2	337	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	337	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
9	333	Gene3D	G3DSA:3.50.50.60	-
9	333	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
264	280	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
293	315	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
9	28	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
138	156	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
177	195	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
155	271	FunFam	G3DSA:3.50.50.60:FF:000014	Dihydrolipoyl dehydrogenase
8	328	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
8	328	InterPro	IPR023753	FAD/NAD(P)-binding domain
42	52	ProSitePatterns	PS00076	Pyridine nucleotide-disulphide oxidoreductases class-I active site.
42	52	InterPro	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site

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 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GJD9	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_2450	ColabFold	—	—	full sequence	—	Loaded

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
33				0.981

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	25.27	0.905
2	3.38	0.121
3	3.27	0.114
4	2.11	0.048
5	2.07	0.046

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
28				0.923
27				0.291

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	26.54	0.915
2	7.35	0.384
3	2.0	0.043
4	1.2	0.011
5	1.15	0.009

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.

71 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
3II	3II4	P9WHH9	625.6 Da LogP 4.65 TPSA 91.4	1 viol.	✓ Clean	`COc1ccc(c(c1)OC)C(=O)N2CCC3(CC2)C(=O)N(CN3c4ccc…`
ACM	1GRF	P00390	59.1 Da LogP -0.51 TPSA 43.1	✓ Ro5	✓ Clean	`CC(=O)N`
AUP	2AAQ	P00390	368.4 Da LogP 6.67 TPSA 25.8	1 viol.	✓ Clean	`c1ccc(cc1)p2c(c3c(c2c4ccccn4)CCCC3)c5ccccn5`
BTB	5NHG	P09622-2	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
ELI	2GH5	P00390	286.3 Da LogP 3.42 TPSA 71.4	✓ Ro5	Alert	`CC1=C(C(=O)c2ccccc2C1=O)CCCCCC(=O)O`
GCG	4GRT	P00390	723.9 Da LogP -4.58 TPSA 313.3	3 viol.	✓ Clean	`C(CCNC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@@H](C(=O)O…`
GDS	2GRT	P00390	612.6 Da LogP -3.88 TPSA 317.6	3 viol.	✓ Clean	`C(CC(=O)N[C@@H](CSSC[C@@H](C(=O)NCC(=O)O)NC(=O)…`
GSH	1DNC	P00390	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`C(CC(=O)N[C@@H](CS)C(=O)NCC(=O)O)[C@@H](C(=O)O)N`
HXP	1XAN	P00390	286.3 Da LogP 3.20 TPSA 87.0	✓ Ro5	✓ Clean	`c1cc2c(cc1O)Oc3cc(ccc3C2CCC(=O)O)O`
MLT	6CMZ	B4EEF2	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
NHE	3RNM	P09622-2	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`
RGS	4GR1	P00390	612.6 Da LogP -3.88 TPSA 317.6	3 viol.	✓ Clean	`C(CNC(=O)[C@@H](CSSC[C@H](C(=O)NCC[C@@H](C(=O)O…`
TS2	3GRT	P00390	721.9 Da LogP -4.04 TPSA 313.3	3 viol.	✓ Clean	`C1CCNC(=O)CNC(=O)[C@H](CSSC[C@@H](C(=O)NCC(=O)N…`
TS4	5GRT	P00390	867.1 Da LogP -4.38 TPSA 377.3	3 viol.	✓ Clean	`C(CCNCCCNC(=O)CNC(=O)[C@H](CSSC[C@@H](C(=O)NCC(…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL1451931	P9WHH9	7.00	263.3 Da LogP 2.58 TPSA 46.2	✓ Ro5	Alert	`O=C1C=C(NCc2ccccc2)c2ccccc2C1=O`
CHEMBL3949128	P9WHH9	6.16	463.7 Da LogP 2.35 TPSA 114.6	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)CN(C)S(=O)(=O)c2cc(Br)cnc2N)cc1Cl`
CHEMBL135536	P00390	6.12	302.3 Da LogP 3.12 TPSA 91.7	✓ Ro5	Alert	`CC1=C(CCCCCC(=O)O)C(=O)c2c(O)cccc2C1=O`
CHEMBL3935059	P9WHH9	6.08	441.4 Da LogP 2.81 TPSA 105.4	✓ Ro5	✓ Clean	`CC(C)c1ccc(NC(=O)CN(C)S(=O)(=O)c2cc(Br)cnc2N)cc1`
CHEMBL3983097	P9WHH9	6.08	459.3 Da LogP 1.70 TPSA 123.9	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)CN(C)S(=O)(=O)c2cc(Br)cnc2N)cc1OC`
M52	P9WHH9	6.02	429.3 Da LogP 1.69 TPSA 114.6	✓ Ro5	✓ Clean	`C[N@@](CC(=O)Nc1ccc(cc1)OC)S(=O)(=O)c2cc(cnc2N)…`
CHEMBL135504	P00390	6.00	288.3 Da LogP 2.73 TPSA 91.7	✓ Ro5	Alert	`CC1=C(CCCCC(=O)O)C(=O)c2c(O)cccc2C1=O`

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
ZINC1615342	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC1710230	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC3830891	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830892	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830893	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC3830894	1.000	307.3 Da LogP -2.21 TPSA 158.8	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS)C(=O)NCC(=O)O)C(=O)O`
ZINC1532230	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556979	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556980	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4556981	0.825	321.4 Da LogP -1.77 TPSA 158.8	✓ Ro5	✓ Clean	`CSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC5828410	0.821	306.3 Da LogP -2.81 TPSA 164.6	1 viol.	✓ Clean	`NC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@H](N)C(=O)O`
ZINC2004372	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC4262829	0.781	263.3 Da LogP 2.74 TPSA 46.2	✓ Ro5	Alert	`O=C1C=C(NCc2ccccc2)C(=O)c2ccccc21`
ZINC13549503	0.780	321.4 Da LogP -2.12 TPSA 147.8	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O`
ZINC4096455	0.775	321.4 Da LogP -1.82 TPSA 158.8	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCCC(=O)O)C(=O)O`
ZINC13522300	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=…`
ZINC31350707	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC…`
ZINC31350710	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(…`
ZINC31350713	0.767	349.4 Da LogP -1.86 TPSA 175.9	✓ Ro5	✓ Clean	`CC(=O)SC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(…`
ZINC3872731	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CSN=O)C(=O)NCC(=O)O)C(=O…`
ZINC3872732	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC3872733	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC3872734	0.767	336.3 Da LogP -1.72 TPSA 188.2	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CSN=O)C(=O)NCC(=O)O)C(=O)O`
ZINC4544082	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544083	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544084	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC4544085	0.767	335.4 Da LogP -1.38 TPSA 158.8	✓ Ro5	✓ Clean	`CCSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC13451235	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C…`
ZINC145953214	0.750	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O…`
ZINC145953600	0.750	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)…`
ZINC14966489	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)C…`
ZINC14966492	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS[C@@H](CC(=O)O)C(=O)O)C(…`
ZINC201224060	0.750	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)…`
ZINC253638410	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS[C@H](CC(=O)O)C(=O)O)C(=…`
ZINC253638411	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS[C@H](CC(=O)O)C(=O)O)C(…`
ZINC2554974	0.750	289.3 Da LogP -1.73 TPSA 158.8	✓ Ro5	✓ Clean	`CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(=O)O`
ZINC3870040	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O`
ZINC3870041	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O`
ZINC3870042	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O`
ZINC3870043	0.750	250.3 Da LogP -1.32 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@H](CCC(=O)N[C@H](CS)C(=O)O)C(=O)O`
ZINC3920510	0.750	423.4 Da LogP -2.47 TPSA 233.4	1 viol.	✓ Clean	`N[C@@H](CCC(=O)N[C@@H](CS[C@@H](CC(=O)O)C(=O)O)…`
ZINC77300920	0.750	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](O)CSC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)N…`
ZINC4556756	0.733	377.4 Da LogP -2.29 TPSA 193.0	✓ Ro5	✓ Clean	`CC(=O)C(=O)SC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)…`
ZINC4556757	0.733	377.4 Da LogP -2.29 TPSA 193.0	✓ Ro5	✓ Clean	`CC(=O)C(=O)SC[C@@H](NC(=O)CC[C@H](N)C(=O)O)C(=O…`
ZINC4556758	0.733	377.4 Da LogP -2.29 TPSA 193.0	✓ Ro5	✓ Clean	`CC(=O)C(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O…`
ZINC4556759	0.733	377.4 Da LogP -2.29 TPSA 193.0	✓ Ro5	✓ Clean	`CC(=O)C(=O)SC[C@@H](NC(=O)CC[C@@H](N)C(=O)O)C(=…`
ZINC504173140	0.733	365.4 Da LogP -2.02 TPSA 179.0	1 viol.	✓ Clean	`C[C@H](CO)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)…`
ZINC5883749	0.733	364.4 Da LogP -2.06 TPSA 187.9	1 viol.	✓ Clean	`CNC(=O)SC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)NCC(…`
ZINC5883754	0.733	364.4 Da LogP -2.06 TPSA 187.9	1 viol.	✓ Clean	`CNC(=O)SC[C@H](NC(=O)CC[C@@H](N)C(=O)O)C(=O)NCC…`

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.