Protein profile

PA2891

geranyl-CoA carboxylase subunit alpha

Genome: NC_002516.2

Gene: PA2891 atuF Structure source: AlphaFold UniProt Q9HZV6

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Amino acids 661

Annotations 5

Features 36

PDB binders 18

Druggability 0.661

Overview

Basic information about this protein and its source genome.

Accession: PA2891
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2891 atuF
Status: annotated
Amino acids: 661
Structure source: AlphaFold

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0004075 Catalysis of the reaction: ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein. GO:0047925 Catalysis of the reaction: ATP + bicarbonate + geranoyl-CoA = 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA + ADP + 2 H+ + phosphate. GO:0046872 Binding to a metal ion. GO:0046247 The chemical reactions and pathways resulting in the breakdown of terpenes, any of a large group of hydrocarbons made up of isoprene units.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 59.574
Human E-value: 2.72e-12
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 0.661

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MPSFNKILVANRGEIACRVLRTAHELGYRSVAVYSEADADTRHVQLADEAVCIGPAAVAQSYLNLEAILDAARRSGAEAIHPGYGFLSENAEFARACEAAGIVFIGPDAEAIHLMGSKRLSKIAMLAAGVPCIPGYEGAEQDDATLRREAERIGYPLMIKASAGGGGRGMRLVEEPGQLLEQLRTARSEALGAFGSAELILERAVLRPRHVEIQVFGDRHGNLLYLGERDCSVQRRHQKVIEEAPCPVLDADLRRAMGEAAVKAAASVNYVGAGTVEFLLGEDGRFYFLEMNTRLQVEHPVTELVTGQDLVAWQIRIAEGHPLPLRQEQVELRGHAIEVRLYAEDAGRGFLPQTGTVLRWDPELLPGVRIDHGLVEGQAVTPFYDPMLAKLIAYGATRDEARRKLIRALERCVLLGVDGNQRFLANLLAHPDFAAGEATTAFIGERFAEDPSLQPRQPGAEELALAAALLYQAGAEASAHQPGLAGWRSAAGAPWKIVLKHAEQRLEIGLEVLESGRRPRLLARLERREIAVRLLDCDGRWASAELDGIRRRHAYHLDGGRLWLYGHGGNLELLDVTHAGASAQVGASSGTLKAPMDGAIVEVLVGEGERVGKGQLLLVLEAMKMEHPLKAGVDGVVRRVQVGRGEQVRNRQVLVEVEADA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0004075 Catalysis of the reaction: ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
GO:0047925 Catalysis of the reaction: ATP + bicarbonate + geranoyl-CoA = 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA + ADP + 2 H+ + phosphate.
GO:0046872 Binding to a metal ion.
GO:0046247 The chemical reactions and pathways resulting in the breakdown of terpenes, any of a large group of hydrocarbons made up of isoprene units.

Sequence Features

Domain/signature hits from InterPro and related databases.

36 records

Show feature table

Start	End	DB	Term	Name
3	448	ProSiteProfiles	PS50979	Biotin carboxylation domain profile.
3	448	InterPro	IPR011764	Biotin carboxylation domain
134	203	FunFam	G3DSA:3.30.1490.20:FF:000003	acetyl-CoA carboxylase isoform X1
584	656	Gene3D	G3DSA:2.40.50.100	-
585	658	SUPERFAMILY	SSF51230	Single hybrid motif
585	658	InterPro	IPR011053	Single hybrid motif
582	658	ProSiteProfiles	PS50968	Biotinyl/lipoyl domain profile.
582	658	InterPro	IPR000089	Biotin/lipoyl attachment
1	450	FunFam	G3DSA:3.30.470.20:FF:000028	Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
85	347	SUPERFAMILY	SSF56059	Glutathione synthetase ATP-binding domain-like
1	133	FunFam	G3DSA:3.40.50.20:FF:000010	Propionyl-CoA carboxylase subunit alpha
1	449	Gene3D	G3DSA:3.30.470.20	-
591	656	Pfam	PF00364	Biotin-requiring enzyme
591	656	InterPro	IPR000089	Biotin/lipoyl attachment
338	444	SMART	SM00878	Biotin_carb_C_2
338	444	InterPro	IPR005482	Biotin carboxylase, C-terminal
4	112	Pfam	PF00289	Biotin carboxylase, N-terminal domain
4	112	InterPro	IPR005481	Biotin carboxylase-like, N-terminal domain
118	324	Pfam	PF02786	Carbamoyl-phosphate synthase L chain, ATP binding domain
118	324	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
333	447	SUPERFAMILY	SSF51246	Rudiment single hybrid motif
333	447	InterPro	IPR011054	Rudiment single hybrid motif
122	319	ProSiteProfiles	PS50975	ATP-grasp fold profile.
122	319	InterPro	IPR011761	ATP-grasp fold
3	479	PANTHER	PTHR18866	CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE
338	444	Pfam	PF02785	Biotin carboxylase C-terminal domain
584	658	FunFam	G3DSA:2.40.50.100:FF:000003	Acetyl-CoA carboxylase biotin carboxyl carrier protein
614	631	ProSitePatterns	PS00188	Biotin-requiring enzymes attachment site.
614	631	InterPro	IPR001882	Biotin-binding site
591	657	CDD	cd06850	biotinyl_domain
155	169	ProSitePatterns	PS00866	Carbamoyl-phosphate synthase subdomain signature 1.
155	169	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
3	115	SUPERFAMILY	SSF52440	PreATP-grasp domain
3	115	InterPro	IPR016185	Pre-ATP-grasp domain superfamily
288	295	ProSitePatterns	PS00867	Carbamoyl-phosphate synthase subdomain signature 2.
288	295	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain

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
AlphaFold PA2891	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
1				0.661

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.

68 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
ACP	4MV8	P43873	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BTI	6YBP	C5AWU5	228.3 Da LogP 0.91 TPSA 58.2	✓ Ro5	✓ Clean	`C1[C@H]2[C@@H]([C@@H](S1)CCCCC=O)NC(=O)N2`
JZK	3JZF	P24182	396.9 Da LogP 4.98 TPSA 72.9	✓ Ro5	✓ Clean	`c1ccc(c(c1)CNc2nc3cc(ccc3n2CC4CCCCC4)C(=O)N)Cl`
JZL	3JZI	P24182	442.0 Da LogP 3.92 TPSA 119.2	✓ Ro5	✓ Clean	`c1ccc(c(c1)CNc2nc3cc(cc(c3n2C[C@@H]4CCCCC[C@@H]…`
L21	2W6Z	P24182	203.2 Da LogP 1.33 TPSA 69.6	✓ Ro5	✓ Clean	`CC(=CCn1cnc(c-2ncnc12)N)C`
L22	2W70	P24182	193.2 Da LogP 0.76 TPSA 90.7	✓ Ro5	✓ Clean	`c1cnc(nc1c2csc(n2)N)N`
L23	2W71	P24182	334.2 Da LogP 3.59 TPSA 69.6	✓ Ro5	✓ Clean	`Cc1nc(cn1Cc2c(cccc2Cl)Cl)c3ccnc(n3)N`
MQM	6OI9	P24182	389.3 Da LogP 3.37 TPSA 94.0	✓ Ro5	✓ Clean	`c1cc(c(c(c1)Cl)c2cc3cnc(nc3nc2N4CC[C@H](C4)CN)N…`
MQV	6OI8	P43873	429.9 Da LogP 3.38 TPSA 106.8	✓ Ro5	✓ Clean	`c1cc(c(c(c1)Cl)c2cc3cnc(nc3nc2N4C[C@@H]5[C@H](C…`
MV4	6OJH	P43873	356.4 Da LogP 2.96 TPSA 94.0	✓ Ro5	✓ Clean	`c1ccc2c(c1)cccc2c3cc4cnc(nc4nc3N5CC[C@H](C5)N)N`
OA1	2W6M	P24182	267.1 Da LogP 2.25 TPSA 69.1	✓ Ro5	✓ Clean	`c1cc(cc(c1)Br)C(=O)c2cnc(o2)N`
OA2	2W6N	P24182	307.4 Da LogP 3.10 TPSA 72.4	✓ Ro5	✓ Clean	`c1ccc(cc1)CN(Cc2ccccc2)C(=O)c3cnc(o3)N`
OA3	2W6O	P24182	191.2 Da LogP 1.21 TPSA 68.9	✓ Ro5	✓ Clean	`CC1(Cc2c(c(ncn2)N)C(=O)C1)C`
OA4	2W6P	P24182	250.3 Da LogP 2.77 TPSA 77.8	✓ Ro5	✓ Clean	`Cc1c(ccc2c1c(nc(n2)N)N)c3ccccc3`
OA5	2W6Q	P24182	247.3 Da LogP 0.49 TPSA 109.2	✓ Ro5	✓ Clean	`c1ccc(cc1)OCCOc2nc(nc(n2)N)N`
PCT	4MV6	P43873	139.0 Da LogP -1.35 TPSA 100.6	✓ Ro5	✓ Clean	`C(C(=O)N)P(=O)(O)O`
PPF	4MV7	P43873	126.0 Da LogP -0.16 TPSA 94.8	✓ Ro5	✓ Clean	`C(=O)(O)P(=O)(O)O`
Y7Y	4RZQ	P43873	316.4 Da LogP 1.36 TPSA 84.9	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@H]1[C@@H]2[C@H](CS1)N(C(=O)N2)C(=…`

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
ZINC2209	1.000	203.2 Da LogP 1.33 TPSA 69.6	✓ Ro5	✓ Clean	`CC(C)=CCn1cnc(N)c2ncnc1-2`
ZINC2557486	1.000	334.2 Da LogP 3.59 TPSA 69.6	✓ Ro5	✓ Clean	`Cc1nc(-c2ccnc(N)n2)cn1Cc1c(Cl)cccc1Cl`
ZINC105469665	0.873	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	0.873	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	0.873	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	0.873	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	0.873	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	0.873	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	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC12360002	0.839	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	0.839	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	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.839	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	0.839	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	0.839	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	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.839	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	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.839	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	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.768	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	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.768	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	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.768	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.768	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	0.768	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	0.768	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	0.754	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.750	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	0.750	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	0.750	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	0.750	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	0.737	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	0.737	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	0.737	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.737	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423	0.726	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC34603442	0.703	215.3 Da LogP 0.28 TPSA 67.1	✓ Ro5	✓ Clean	`NCCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC5615251	0.700	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	0.700	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	0.700	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	0.700	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…`
ZINC31516918	0.692	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…`
ZINC5486730	0.689	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`

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.