Protein profile

KP13_04825

High-molecular-weight protein 1

Genome: KpKP13

Gene: AHE43792.1 irp1 Structure source: Unavailable UniProt A0A0H3GQF9

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Amino acids 3163

Annotations 13

Features 96

PDB binders 9

Overview

Basic information about this protein and its source genome.

Accession: KP13_04825
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43792.1 irp1
Status: annotated
Amino acids: 3163
Structure source: Unavailable

GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor). GO:0004315 Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]. GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones. GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate). GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 31.071
Human E-value: 1.59e-25
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: CytoplasmicMembrane

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 4 / 4744 genomes with a hit

Normalized 0.001

Sequence

Primary amino-acid sequence viewer.

MDNLRFSSAPTADSIDASIAQHYPDCEPVAVIGYACHFPESPDGETFWQNLLEGRECSRRFTREELLAVGLDAAIIDDPHYVNIGTVLDNADCFDATLFGYSRQEAESMDPQQRLFLQAVWHALEHAGYAPGAVPHKTGVFASSRMSTYPGREALNVTEVAQVKGLQSLMGNDKDYIATRAAYKLNLHGPALSVQTACSSSLVAVHLACESLRAGESDMAVAGGVALSFPQQAGYRYQPGMIFSPDGHCRPFDASAEGTWAGNGLGCVVLRRLRDALLSGDPIISVILSSAVNNDGNRKVGYTAPSVAGQQAVIEEALMLAAIDDRQVGYIETHGTGTPLGDAIEIEALRNVYAPRPQDQRCALGSVKSNMGHLDTAAGIAGLLKTVLAVSRGQIPPLLNFHTPNPALKLEESPFTIPVSAQAWQDEMRYAGVSSFGIGGTNCHMIVASLPDALNARLPNTDSGRKSTALLLSAASDSALRRLATDYAGALRENADASSLAFTALHARRLDLPFRLAAPLNRETAEALSAWAGEKSGALVYSGHGASGKQVWLFTGQGSHWRTMGQTMYQHSTAFADTLDRCFSACSEMLTPSLREAMFNPDSAQLDNMAWAQPAIVAFEIAMAAHWRAEGLKPDFAIGHSVGEFAAAVVCGHYTIEQVMPLVCRRGALMQQCASGAMVAVFADEDTLMPLARQFELDLAANNGTQHTVFSGPEAHLAVFCATLSQHDINYRRLSVTGAAHSALLEPILDRFQDACAGLHAEPGQIPIISTLTADVIDESTLNQADYWRRHMRQPVRFIQSIQVAHQLGARVFLEMGPDAQLVACGQREYRDNAYWIASARRNKEASDVLNQALLQLYAAGVALPWADLLAGDGQRIAAPCYPFDTERYWKERVSPACEPADAALSAGLEVASRAATALDLPRLEALKQCATRLHAIYVDQLVQRCTGDAIENGVDAMTIMRRGRLLPRYQQLLQRLLNNCVVDGDYRCTDGRYVRARPIEHQQRESLLTELAGYCEGFQAIPDTIARAGDRLYEMMSGAEEPVAIIFPQSASDGVEVLYQEFSFGRYFNQIAAGVLRGIVQTRQPRQPLRILEVGGGTGGTTAWLLPELNGVPALEYHFTDISALFTRRAQQKFADYDFVKYSELDLEKEAQSQGFQAQSYDLIVAANVIHATRHIGRTLDNLRPLLKPGGRLLMREITQPMRLFDFVFGPLVLPLQDLDAREGELFLTTAQWQQQCRHAGFSKVAWLPQDGSPTAGMSEHIILATLPGQAVSAVTFTAPSEPVLGQALTDNGDYLADWSDCAGQPERFNARWQEAWRLLSQRHGDALPVEPPPVAAPEWLGKVRLSWQNEAFSRGQMRVEARHPAGEWLPLSPAAPLPAPQTHYQWRWTPLNVASIDHPLTFSFSAGTLARSDELAQYGIIHDPHASSRLMIVEESEDTLALAEKVIAALTASAAGLIVVTRRAWRVEENEALSASHHALWALLRVAANEQPERLLAAIDLAENTPWETLHQGLSAVSLSQRWLAARGDTLWLPSLAPNTGCAAELPANVFTGDSRWHLVTGAFGGLGRLAVNWLREKGARRIALLAPRVDESWLRDVEGGQTRVCRCDVGDAGQLATVLDDLAANGGIAGAIHAAGVLADAPLQELDDHQLAAVFAVKAQAASQLLQTLRNHDGRYLILYSSAAATLGAPGQSAHALACGYLDGLAQQFSTLDAPKTLSVAWGAWGESGRAATPEMLATLASRGMGALSDAEGCWHLEQAVMRGAPWRLAMRVFTDKMPPLQQALFNISATEKAATPVIPPADDNAFNGSLSDETAVMAWLKKRIAVQLRLSDPASLHPNQDLLQLGMDSLLFLELSSDIQHYLGVRINAERAWQDLSPHGLTQLICSKPEATPAASQPEVLRHDADERYAPFPLTPIQHAYWLGRTHLIGYGGVACHVLFEWDKRHDEFDLAILEKAWNQLIARHDMLRMVVDADGQQRILATTPEYHIPRDDLRALSPEEQRIALEKRRHELSYRVLPADQWPLFELVVSEIDDCHYRLHMNLDLLQFDVQSFKVMMDDLAQVWRGETLAPLAITFRDYVMAEQARRQTSAWHDAWDYWQEKLPQLPLAPELPVVETPPETPHFTTFKSTIGKTEWQAVKQRWQQQGVTPSAALLTLFAATLERWSRTTTFTLNLTFFNRQPIHPQINQLIGDFTSVTLVDFNFSAPVTLQEQMQQTQQRLWQNMAHSEMNGVEVIRELGRLRGSQRQPLMPVVFTSMLGMTLEGMTIDQAMSHLFGEPCYVFTQTPQVWLDHQVMESDGELMFSWYCMDNVLEPGAAEAMFNDYCAILQAVIAAPESLKTLTSGIAGHIPRRRWPLNAQADYDLRDIEQATLEYPGIRQARAEITEQGALTLDIVMADDPSPSAAMPDEHELTQLALPLPEQAQLDELEATWRWLEARALQGIAATLNRHGLFTTPEIAHRFSAIVQALSAQASHQRLLRQWLQCLTEREWLIREGESWRCRIPLSEIPEPQEACPQSQWSQALAQYLETCIARHDALFSGQCSPLELLFNEQHRVTDALYRDNPASACLNRYTAQIAALCSAERILEVGAGTAATTAPVLKATRNTRQSYHFTDVSAQFLNDARARFHDESQVSYALFDINQPLDFTAHPEAGYDLIVAVNVLHDASHVVQTLRRLKLLLKAGGRLLIVEATERNSVFQLASVGFIEGLSGYRDFRRRDEKPMLTRSAWQEVLVQAGFANELAWPAQESSPLRQHLLVARSPGVNRPDKKAVSRYLQQRFGTGLPILQIRQREALFTPLHAPSDAPTEPAKPTPVAGGNPALEKQVAELWQSLLSRPVARHHDFFELGGDSLMATRMVAQLNRRGIARANLQDLFSHSTLSDFCAHLQAATSGEDNPIPLCQGDGEETLFVFHASDGDISAWLPLASALNRRVFGLQAKSPQRFATLDQMIDEYVGCIRRQQPHGPYVLAGWSYGAFLAAGAAQRLYAKGEQVRMVLIDPVCRQDFCCENRAALLRLLAEGQTPLALPEHFDQQTPDSQLADFISLAKTAGMVSQNLTLQAAETWLDNIAHLLRLLTEHTPGESVPVPCLMVYAAGRPARWTPAETEWQGWINNADDAVIEASHWQIMMEAPHVQACAQHITRWLCATSTQPENSL

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

13 GO

Gene Ontology (GO)

GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
GO:0004315 Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0004312 Catalysis of the reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H+ = long-chain fatty acid + n+1 CoA + n CO2 + 2n NADP+.
GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
GO:0071770 The aggregation, arrangement and bonding together of a set of components, including (phenyl)phthiocerol, phthiodiolone, phthiotriol dimycocerosate and diphthioceranate, to form the DIM/DIP layer of the Actinobacterium-type cell wall.
GO:0009403 The chemical reactions and pathways resulting in the formation of toxin, a poisonous compound (typically a protein) that is produced by cells or organisms and that can cause disease when introduced into the body or tissues of an organism.

Sequence Features

Domain/signature hits from InterPro and related databases.

96 records

Show feature table

Start	End	DB	Term	Name
551	846	Pfam	PF00698	Acyl transferase domain
551	846	InterPro	IPR014043	Acyl transferase
1948	2263	Pfam	PF00668	Condensation domain
1948	2263	InterPro	IPR001242	Condensation domain
2575	2750	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
2575	2750	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
1560	1729	Pfam	PF08659	KR domain
1560	1729	InterPro	IPR013968	Polyketide synthase, ketoreductase domain
3163	3163	Coils	Coil	Coil
551	847	Gene3D	G3DSA:3.40.366.10	-
551	847	InterPro	IPR001227	Acyl transferase domain superfamily
2824	2898	ProSiteProfiles	PS50075	Carrier protein (CP) domain profile.
2824	2898	InterPro	IPR009081	Phosphopantetheine binding ACP domain
1557	1786	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
1557	1786	InterPro	IPR036291	NAD(P)-binding domain superfamily
2813	2902	Gene3D	G3DSA:1.10.1200.10	-
2813	2902	InterPro	IPR036736	ACP-like superfamily
550	835	SUPERFAMILY	SSF52151	FabD/lysophospholipase-like
550	835	InterPro	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase
997	1255	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
997	1255	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
2444	2767	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
2444	2767	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
27	447	CDD	cd00833	PKS
2096	2343	FunFam	G3DSA:3.30.559.30:FF:000006	Yersiniabactin polyketide/non-ribosomal peptide synthetase
19	473	Gene3D	G3DSA:3.40.47.10	-
19	473	InterPro	IPR016039	Thiolase-like
1823	1889	Pfam	PF00550	Phosphopantetheine attachment site
1823	1889	InterPro	IPR009081	Phosphopantetheine binding ACP domain
2832	2894	Pfam	PF00550	Phosphopantetheine attachment site
2832	2894	InterPro	IPR009081	Phosphopantetheine binding ACP domain
1818	1902	Gene3D	G3DSA:1.10.1200.10	-
1818	1902	InterPro	IPR036736	ACP-like superfamily
2905	3157	Gene3D	G3DSA:3.40.50.1820	alpha/beta hydrolase
2905	3157	InterPro	IPR029058	Alpha/Beta hydrolase fold
27	276	Pfam	PF00109	Beta-ketoacyl synthase, N-terminal domain
27	276	InterPro	IPR014030	Beta-ketoacyl synthase, N-terminal
2095	2347	Gene3D	G3DSA:3.30.559.30	Nonribosomal peptide synthetase, condensation domain
1435	1776	CDD	cd05274	KR_FAS_SDR_x
285	401	Pfam	PF02801	Beta-ketoacyl synthase, C-terminal domain
285	401	InterPro	IPR014031	Beta-ketoacyl synthase, C-terminal
2918	3152	SMART	SM00824	Thioesterase
2918	3152	InterPro	IPR020802	Polyketide synthase, thioesterase domain
2853	2868	ProSitePatterns	PS00012	Phosphopantetheine attachment site.
2853	2868	InterPro	IPR006162	Phosphopantetheine attachment site
1910	2088	FunFam	G3DSA:3.30.559.10:FF:000023	Non-ribosomal peptide synthetase
2830	2898	SMART	SM00823	Phosphopantetheine attachment site
2830	2898	InterPro	IPR020806	Polyketide synthase, phosphopantetheine-binding domain
1821	1893	SMART	SM00823	Phosphopantetheine attachment site
1821	1893	InterPro	IPR020806	Polyketide synthase, phosphopantetheine-binding domain
2098	2343	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
1818	1893	ProSiteProfiles	PS50075	Carrier protein (CP) domain profile.
1818	1893	InterPro	IPR009081	Phosphopantetheine binding ACP domain
1435	1455	Coils	Coil	Coil
1915	2341	CDD	cd19535	Cyc_NRPS
1911	2109	SUPERFAMILY	SSF52777	CoA-dependent acyltransferases
1558	1731	SMART	SM00822	This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
2828	2894	SUPERFAMILY	SSF47336	ACP-like
2828	2894	InterPro	IPR036736	ACP-like superfamily
189	205	ProSitePatterns	PS00606	Ketosynthase family 3 (KS3) active site signature.
189	205	InterPro	IPR018201	Beta-ketoacyl synthase, active site
2915	3006	Pfam	PF00975	Thioesterase domain
2915	3006	InterPro	IPR001031	Thioesterase
26	449	ProSiteProfiles	PS52004	Ketosynthase family 3 (KS3) domain profile.
26	449	InterPro	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain
1093	1194	Pfam	PF08242	Methyltransferase domain
1093	1194	InterPro	IPR013217	Methyltransferase type 12
2593	2693	Pfam	PF08242	Methyltransferase domain
2593	2693	InterPro	IPR013217	Methyltransferase type 12
1762	3021	PANTHER	PTHR43775	FATTY ACID SYNTHASE
1848	1863	ProSitePatterns	PS00012	Phosphopantetheine attachment site.
1848	1863	InterPro	IPR006162	Phosphopantetheine attachment site
1366	1540	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
1366	1540	InterPro	IPR036291	NAD(P)-binding domain superfamily
29	452	SMART	SM00825	Beta-ketoacyl synthase
29	452	InterPro	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain
1817	1928	SUPERFAMILY	SSF47336	ACP-like
1817	1928	InterPro	IPR036736	ACP-like superfamily
2898	3152	SUPERFAMILY	SSF53474	alpha/beta-Hydrolases
2898	3152	InterPro	IPR029058	Alpha/Beta hydrolase fold
474	890	Gene3D	G3DSA:3.30.70.3290	-
23	496	FunFam	G3DSA:3.40.47.10:FF:000042	Polyketide synthase Pks13
23	447	SUPERFAMILY	SSF53901	Thiolase-like
23	447	InterPro	IPR016039	Thiolase-like
675	736	SUPERFAMILY	SSF55048	Probable ACP-binding domain of malonyl-CoA ACP transacylase
675	736	InterPro	IPR016036	Malonyl-CoA ACP transacylase, ACP-binding
404	515	Pfam	PF16197	Ketoacyl-synthetase C-terminal extension
404	515	InterPro	IPR032821	Polyketide synthase, C-terminal extension
2805	2826	MobiDBLite	mobidb-lite	consensus disorder prediction
1910	2090	Gene3D	G3DSA:3.30.559.10	-
1910	2090	InterPro	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily
1345	1795	Gene3D	G3DSA:3.40.50.720	-
1060	1250	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
1060	1250	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
553	844	SMART	SM00827	Acyl transferase domain in polyketide synthase (PKS) enzymes.
553	844	InterPro	IPR014043	Acyl transferase

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.

59 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
57H	5D3Z	Q03133	122.1 Da LogP 0.35 TPSA 57.5	✓ Ro5	✓ Clean	`C=CCP(=O)(O)O`
8H6	5XWV	Q93NW7	390.5 Da LogP -0.14 TPSA 132.8	✓ Ro5	✓ Clean	`CCC(=O)[C@@H](C)C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(…`
AKG	3NNF	Q6DNF2	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
DUV	5YDL	A0A0E3JLZ0	154.2 Da LogP 0.69 TPSA 54.4	✓ Ro5	✓ Clean	`C#CCCCC(C=O)C(=O)O`
DUW	5YDM	A0A0E3JLZ0	178.2 Da LogP 1.13 TPSA 54.4	✓ Ro5	✓ Clean	`c1ccc(cc1)C[C@H](C=O)C(=O)O`
E5U	6L3M	Q8KUH4	134.1 Da LogP -0.83 TPSA 83.8	✓ Ro5	✓ Clean	`COC(C(=O)O)C(=O)O`
LMR	3MJS	Q93NW7	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)O)C(=O)O`
MLT	3MJS	Q93NW7	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
PNS	2LIW	Q6DNF2	358.4 Da LogP -0.96 TPSA 145.2	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)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
ZINC71773889	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O`
ZINC71773890	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC71773891	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC31938448	0.656	266.3 Da LogP 3.25 TPSA 34.1	✓ Ro5	✓ Clean	`O=C[C@@H](Cc1ccccc1)C(=O)CCc1ccccc1`
ZINC31938449	0.656	266.3 Da LogP 3.25 TPSA 34.1	✓ Ro5	✓ Clean	`O=C[C@H](Cc1ccccc1)C(=O)CCc1ccccc1`
ZINC3869683	0.643	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@H](O)C(=O)NCCC(=O)NCCS`
ZINC3869684	0.643	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@@H](O)C(=O)NCCC(=O)NCCS`
ZINC73739659	0.636	206.2 Da LogP 1.61 TPSA 43.4	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](C=O)Cc1ccccc1`
ZINC73739661	0.636	206.2 Da LogP 1.61 TPSA 43.4	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H](C=O)Cc1ccccc1`
ZINC27644247	0.618	230.3 Da LogP 0.09 TPSA 111.2	✓ Ro5	✓ Clean	`CCCCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC196899382	0.588	228.2 Da LogP -0.14 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CCCNC(=O)C(F)(F)F)C(=O)O`
ZINC4155291	0.583	216.2 Da LogP -1.37 TPSA 130.8	✓ Ro5	✓ Clean	`CC(=O)/N=C(\N)NCCC[C@H](N)C(=O)O`
ZINC4155299	0.583	216.2 Da LogP -1.37 TPSA 130.8	✓ Ro5	✓ Clean	`CC(=O)/N=C(\N)NCCC[C@@H](N)C(=O)O`
ZINC1529718	0.571	202.3 Da LogP -0.74 TPSA 102.4	✓ Ro5	✓ Clean	`CN(C)C(=N)NCCC[C@H](N)C(=O)O`
ZINC1546170	0.571	216.3 Da LogP -0.30 TPSA 111.2	✓ Ro5	✓ Clean	`CCCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC1693352	0.571	240.3 Da LogP 3.17 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)C(Cc1ccccc1)Cc1ccccc1`
ZINC2560273	0.571	202.3 Da LogP -0.69 TPSA 111.2	✓ Ro5	✓ Clean	`CCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC35874629	0.571	224.3 Da LogP 3.29 TPSA 17.1	✓ Ro5	✓ Clean	`O=CC(Cc1ccccc1)Cc1ccccc1`
ZINC4543782	0.571	202.3 Da LogP -0.74 TPSA 102.4	✓ Ro5	✓ Clean	`CN(C)C(=N)NCCC[C@@H](N)C(=O)O`
ZINC7997269	0.571	205.3 Da LogP 0.07 TPSA 99.2	✓ Ro5	✓ Clean	`CSC(=N)NCCC[C@@H](N)C(=O)O`
ZINC144076260	0.559	232.2 Da LogP -0.84 TPSA 129.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC(=O)O)C(=O)O`
ZINC218922593	0.559	204.2 Da LogP -1.32 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CO)C(=O)O`
ZINC2516116	0.559	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC4545887	0.559	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC4545888	0.559	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)NCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC4545889	0.559	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC50027904	0.559	261.3 Da LogP -1.51 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC12503853	0.556	201.3 Da LogP 0.55 TPSA 99.2	✓ Ro5	✓ Clean	`CCCC(=N)NCCC[C@H](N)C(=O)O`
ZINC1640080	0.556	232.3 Da LogP 0.70 TPSA 101.6	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)NCCC[C@H](N)C(=O)O`
ZINC217503161	0.556	230.3 Da LogP 0.88 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCC(=O)NCCCC[C@H](N)C(=O)O`
ZINC2560765	0.556	232.3 Da LogP 0.70 TPSA 101.6	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)NCCC[C@@H](N)C(=O)O`
ZINC3055005	0.556	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007	0.556	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010	0.556	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC675038108	0.556	231.3 Da LogP -1.49 TPSA 123.3	1 viol.	✓ Clean	`CNC(NC)C(=N)NCCC[C@H](N)C(=O)O`
ZINC100017163	0.553	213.3 Da LogP 0.71 TPSA 99.2	✓ Ro5	✓ Clean	`C/C=C/CC(=N)NCCC[C@H](N)C(=O)O`
ZINC19796052	0.553	219.2 Da LogP -1.73 TPSA 156.9	✓ Ro5	✓ Clean	`N/C(=N\[N+](=O)[O-])NCCC[C@H](N)C(=O)O`
ZINC21982226	0.553	219.2 Da LogP -1.73 TPSA 156.9	✓ Ro5	✓ Clean	`N/C(=N\[N+](=O)[O-])NCCC[C@@H](N)C(=O)O`
ZINC5113209	0.548	275.3 Da LogP -0.26 TPSA 138.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC13545298	0.543	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCC(=O)NCCCC[C@H](N)C(=O)O`
ZINC216616240	0.543	430.5 Da LogP 0.72 TPSA 184.8	1 viol.	✓ Clean	`N[C@@H](CCCCNC(=O)CCCCCCC(=O)NCCCC[C@H](N)C(=O)…`
ZINC6360447	0.543	222.3 Da LogP 0.37 TPSA 75.3	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=S)S)C(=O)O`
ZINC1530092	0.541	254.2 Da LogP -1.61 TPSA 168.8	1 viol.	✓ Clean	`N=C(NCCC[C@H](N)C(=O)O)NP(=O)(O)O`
ZINC230402790	0.541	214.3 Da LogP 0.26 TPSA 92.4	✓ Ro5	✓ Clean	`C/C=C/C(=O)NCCCC[C@H](N)C(=O)O`
ZINC237993466	0.541	214.3 Da LogP 0.26 TPSA 92.4	✓ Ro5	✓ Clean	`C/C=C/C(=O)NCCCC[C@@H](N)C(=O)O`
ZINC2509855	0.541	216.2 Da LogP 0.09 TPSA 101.6	✓ Ro5	✓ Clean	`C=CCOC(=O)NCCC[C@H](N)C(=O)O`
ZINC5965908	0.541	202.3 Da LogP -1.03 TPSA 99.7	✓ Ro5	✓ Clean	`C/N=C(\NC)NCCC[C@H](N)C(=O)O`
ZINC98044182	0.541	216.2 Da LogP 0.09 TPSA 101.6	✓ Ro5	✓ Clean	`C=CCOC(=O)NCCC[C@@H](N)C(=O)O`
ZINC1555366	0.536	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1555369	0.536	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`

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.

3D Structure

No structural model is available for this protein.

Structure unavailable

No pre-computed model was found in the AlphaFold database and no ColabFold prediction is available for this protein.

Sequence length: 3163 aa