Protein profile

PA4403

preprotein translocase subunit SecA

Genome: NC_002516.2

Gene: PA4403 secA Structure source: AlphaFold UniProt Q9LCT3

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Amino acids 916

Annotations 13

Features 63

PDB binders 4

Druggability 0.643

Overview

Basic information about this protein and its source genome.

Accession: PA4403
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4403 secA
Status: annotated
Amino acids: 916
Structure source: AlphaFold

7.4.2.8

GO:0031522 A transmembrane protein complex involved in the translocation of proteins across the cytoplasmic membrane. In Gram-negative bacteria, Sec-translocated proteins are subsequently secreted via the type II, IV, or V secretion systems. Sec complex components include SecA, D, E, F, G, Y and YajC. 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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0046872 Binding to a metal ion. GO:0008564 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + protein+(in) = ADP + phosphate + protein+(out); drives the concomitant secretion of proteins.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

Selected Druggability evidence

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 0.643

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MFAPLLKKLFGSKNERDVKRMAKAVQAINALEPQMVALSDEQLKAKTAEFQQRYAKGETLDQLLPEAFAVVREAGKRVMGMRHFDVQLIGGMTLHDGKIAEMRTGEGKTLVGTLPVYLNALSGKGVHVVTVNDYLARRDANWMRPLYEFLGLSVGVVTPFQPPEDKRAAYAADITYGTNNEFGFDYLRDNMAFSLDDKFQRELNFAVVDEVDSILIDEARTPLIISGQAEDSSELYIKINKLIPRLKRQVEEVEGKPTEEGHYSIDEKTRQVELNEQGHQFIEDLLSQNGLLGEGESLYSAHNLSLLTHVYAALRAHTLFHRNVEYIVQGDQILLIDEHTGRTMPGRRLSEGLHQAIEAKEGLPIQAESQTLASTTFQNYFRLYNKLAGMTGTADTEAFEFRQIYGLDVVVIPTHRPIARKDFNDLVYLTQEEKYAAIITDIKQCQALGRPILVGTASIESSEYVSKLLQEAGIEHKVLNAKYHEKEAEIIAQAGAPGSVTIATNMAGRGTDILLGGNWEVEVAALENPTEEQIAQIKAEWQKRHQQVIEAGGLHVIASERHESRRIDNQLRGRAGRQGDPGSSRFYLSLEDNLMRIFASDRVKNFMKALGMQSGEAIEHRMVTNAIEKAQRKVEGRNFDIRKQLLEFDDVANEQRKVIYHMRNTLLSAEDVGETIKEFREETLSATINQHIPPQSLPEQWDIEGLEAALYSDFAVRLPIQQWLDEDDKLYEETLRSKILEQIVAAYYEKEELAGAEALRAFEKQMLLRVLDDLWKDHLSTMDHLRHGIHLRGYAQKNPKQEYKRESFTLFQELLDSIKRDTIRVLSHVQVRREDPAEEEARLRREAEELAKRMQFQHAEAPSMEQAVAGEEEELPEGPAPVVPLEPVRNEQKIGRNEPCPCGSGKKYKHCHGQLD

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Enzyme Commission (EC)

7.4.2.8

Gene Ontology (GO)

GO:0031522 A transmembrane protein complex involved in the translocation of proteins across the cytoplasmic membrane. In Gram-negative bacteria, Sec-translocated proteins are subsequently secreted via the type II, IV, or V secretion systems. Sec complex components include SecA, D, E, F, G, Y and YajC.
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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0046872 Binding to a metal ion.
GO:0008564 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + protein+(in) = ADP + phosphate + protein+(out); drives the concomitant secretion of proteins.
GO:0065002 The directed movement of proteins in a cell, from one side of a membrane to another by means of some agent such as a transporter or pore.
GO:0017038 The targeting and directed movement of proteins into a cell or organelle. Not all import involves an initial targeting event.
GO:0006605 The process of targeting specific proteins to particular regions of the cell, typically membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif.
GO:0043952 The process in which unfolded proteins are transported across the cytoplasmic membrane in Gram-positive and Gram-negative bacteria by the Sec complex, in a process involving proteolytic cleavage of an N-terminal signal peptide.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0006886 The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.

Sequence Features

Domain/signature hits from InterPro and related databases.

63 records

Show feature table

Start	End	DB	Term	Name
42	414	CDD	cd17928	DEXDc_SecA
21	246	FunFam	G3DSA:3.40.50.300:FF:000081	Preprotein translocase subunit SecA
89	247	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
89	247	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
840	860	Coils	Coil	Coil
857	916	MobiDBLite	mobidb-lite	consensus disorder prediction
229	368	FunFam	G3DSA:3.90.1440.10:FF:000001	Preprotein translocase subunit SecA
617	830	Pfam	PF07516	SecA Wing and Scaffold domain
617	830	InterPro	IPR011116	SecA Wing/Scaffold
417	620	FunFam	G3DSA:3.40.50.300:FF:000113	Preprotein translocase subunit SecA
417	620	Gene3D	G3DSA:3.40.50.300	-
417	620	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
621	833	FunFam	G3DSA:1.10.3060.10:FF:000001	Preprotein translocase subunit SecA
5	415	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
5	415	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
5	871	PANTHER	PTHR30612	SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM
5	871	InterPro	IPR000185	Protein translocase subunit SecA
896	913	Pfam	PF02810	SEC-C motif
896	913	InterPro	IPR004027	SEC-C motif
621	833	Gene3D	G3DSA:1.10.3060.10	Helical scaffold and wing domains of SecA
231	370	Gene3D	G3DSA:3.90.1440.10	-
228	358	SMART	SM00958	SecA_PP_bind_2
228	358	InterPro	IPR011130	SecA, preprotein cross-linking domain
416	618	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
416	618	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
3	619	ProSiteProfiles	PS51196	SecA family profile.
3	619	InterPro	IPR014018	SecA motor DEAD
28	818	NCBIfam	TIGR00963	preprotein translocase subunit SecA
28	818	InterPro	IPR000185	Protein translocase subunit SecA
469	489	Coils	Coil	Coil
170	190	PRINTS	PR00906	SecA protein signature
170	190	InterPro	IPR000185	Protein translocase subunit SecA
63	87	PRINTS	PR00906	SecA protein signature
63	87	InterPro	IPR000185	Protein translocase subunit SecA
376	393	PRINTS	PR00906	SecA protein signature
376	393	InterPro	IPR000185	Protein translocase subunit SecA
101	115	PRINTS	PR00906	SecA protein signature
101	115	InterPro	IPR000185	Protein translocase subunit SecA
117	127	PRINTS	PR00906	SecA protein signature
117	127	InterPro	IPR000185	Protein translocase subunit SecA
339	361	PRINTS	PR00906	SecA protein signature
339	361	InterPro	IPR000185	Protein translocase subunit SecA
413	426	PRINTS	PR00906	SecA protein signature
413	426	InterPro	IPR000185	Protein translocase subunit SecA
422	635	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
422	635	InterPro	IPR001650	Helicase, C-terminal
6	402	SMART	SM00957	SecA_DEAD_2
6	402	InterPro	IPR011115	SecA DEAD-like, N-terminal
23	416	Gene3D	G3DSA:3.40.50.300	-
23	416	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
420	589	CDD	cd18803	SF2_C_secA
420	589	InterPro	IPR044722	SecA, C-terminal helicase domain
620	904	SUPERFAMILY	SSF81886	Helical scaffold and wing domains of SecA
620	904	InterPro	IPR036266	SecA, Wing/Scaffold superfamily
6	402	Pfam	PF07517	SecA DEAD-like domain
500	515	ProSitePatterns	PS01312	SecA family signature.
500	515	InterPro	IPR020937	SecA conserved site
5	832	Hamap	MF_01382	Protein translocase subunit SecA [secA].
5	832	InterPro	IPR000185	Protein translocase subunit SecA
232	358	Pfam	PF01043	SecA preprotein cross-linking domain
232	358	InterPro	IPR011130	SecA, preprotein cross-linking domain
227	368	SUPERFAMILY	SSF81767	Pre-protein crosslinking domain of SecA
227	368	InterPro	IPR036670	SecA, preprotein cross-linking domain superfamily

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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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
AlphaFold PA4403	AlphaFold	—	—	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
4				0.626
20				0.55
3				0.513
26				0.418

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.

54 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
AGS	6T4H	Q183M9	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP	2FSH	P10408	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BEF	5EUL	P28366	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
PGV	6ITC	P28366	749.0 Da LogP 10.45 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OC[C@H…`

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
ZINC102191119	0.875	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC58649551	0.875	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC12360002	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC31977053	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC16546165	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC13518964	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224	0.768	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423	0.738	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC31516918	0.730	446.4 Da LogP -1.33 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…`
ZINC105469665	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC5615251	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615253	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC5615258	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615263	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC14880758	0.700	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC62592204	0.700	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC…`

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.