Protein profile

KP13_00823

Phosphoribosylformylglycinamidine synthase

Genome: KpKP13

Gene: AHE43187.1 purL Structure source: AlphaFold + ColabFold UniProt A0A0H3GWU2

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Amino acids 1295

Annotations 6

Features 48

PDB binders 4

Druggability 0.899

Overview

Basic information about this protein and its source genome.

Accession: KP13_00823
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43187.1 purL
Status: annotated
Amino acids: 1295
Structure source: AlphaFold + ColabFold

6.3.5.3

GO:0006189 The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate. GO:0004642 Catalysis of the reaction: N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + ATP + H2O = 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate + ADP + 2 H+ + phosphate. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0046872 Binding to a metal ion.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 46.512
Human E-value: 1.55e-06
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 65.405
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 97.28

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 0.899

Structure A0A0H3GWU2

Pocket Pocket 4

P2Rank 0.99

Structure A0A0H3GWU2

Pocket Pocket 1

ColabFold model

FPocket 0.905 · Pocket 23

P2Rank 0.991 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 256 / 4744 genomes with a hit

Normalized 0.054

Sequence

Primary amino-acid sequence viewer.

MMEILRGSPALSAFRINKLLARFQAANLPVSAIYAEYIHFADLNAPLSADDRERLARLLQYGPSLSSHTPTGKLLLVTPRPGTISPWSSKATDIAHNCGLAQVVRLERGVAYYVEASTLTEAQWAAVAAELHDRMMESVFDELEAGEKLFAHHQPTPVTSVDLLGEGRQALIDANLRLGLALADDEIDYLQDAFTRLGRNPNDIELYMFAQANSEHCRHKIFNADWIIDGEQQPKSLFKMIKNTFEKTPDYVLSAYKDNAAVMEGSEVGRYFADHQTGRYDFHQEPAHILMKVETHNHPTAISPWPGAATGSGGEIRDEGATGRGAKPKAGLVGFSVSNLRIPGFEQPWEEDFGKPDRIVTALDIMTEGPLGGAAFNNEFGRPALNGYFRTYEEKVTSHNGEELRGYHKPIMLAGGIGNIRGEHVQKGEITVGAKLIVLGGPAMNIGLGGGAASSMASGQSDADLDFASVQRDNPEMERRCQEVIDRCWQLGDANPILFIHDVGAGGLSNAMPELVSDGGRGGKFQLRDILSDEPGMSPLEIWCNESQERYVLAVAPEQLPLFDELCRRERAPYAVIGEATAEQHLSLSDSHFNDQPIDLPLDVLLGKTPKMTRDVQTLKAQGSALDRQPIILADAVNRVLHLPTVAEKTFLVTIGDRTVTGMVARDQMVGPWQIPVANCAVTTASLDSYYGEAMAMGERAPVALLDFAASGRLAVGEALTNIAATQIGELNRVKLSANWMAAAGHPGEDAGLYEAVKAVGEELCPALGLTIPVGKDSMSMKTRWQEGSEQREMTSPLSLVISAFARVEDVRHTVTPQLSTEDNALLLIDLGKGHNALGATALAQVYRQLGDKPADVRDVAQLKGFWNAMQALVAQRKLLAYHDRSDGGLLVTLAEMAFTGHCGVEADIAALGDDHLAALFNEELGAVIQVRAADREAVEAILAVNGLADCVHYLGKAVEGDRFVLTAGGQTVFSESRTTLRMWWAETTWQMQRLRDNPACADQEHEAKANDADPGLNVKLSFDINDDVAAPYIATGARPKVAVLREQGVNSHVEMAAAFHRAGFDAIDVHMSDLLAGRTGLGDFHALVACGGFSYGDVLGAGEGWAKSILFNERVRDEFATFFHRPQTLALGVCNGCQMMSNLRELIPGSDLWPRFVRNQSDRFEARFSLVEVTQSPSLLLEGMVGSRMPIAVSHGEGQVEVRDSAHLAQLESKGLVALRFVDNFGKVTETYPANPNGSPNGITAVTSESGRATIMMPHPERVFRTVSNSWHPENWGEDSPWMRIFRNARKQLG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

6.3.5.3

Gene Ontology (GO)

GO:0006189 The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
GO:0004642 Catalysis of the reaction: N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + ATP + H2O = 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate + ADP + 2 H+ + phosphate.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0046872 Binding to a metal ion.

Sequence Features

Domain/signature hits from InterPro and related databases.

48 records

Show feature table

Start	End	DB	Term	Name
4	1293	NCBIfam	TIGR01735	phosphoribosylformylglycinamidine synthase
4	1293	InterPro	IPR010073	Phosphoribosylformylglycinamidine synthase PurL
1039	1294	SMART	SM01211	GATase_5_2
155	220	SUPERFAMILY	SSF109736	FGAM synthase PurL, linker domain
1042	1291	CDD	cd01740	GATase1_FGAR_AT
1	152	SUPERFAMILY	SSF82697	PurS-like
1	152	InterPro	IPR036604	Phosphoribosylformylglycinamidine synthase subunit PurS-like superfamily
214	420	FunFam	G3DSA:3.30.1330.10:FF:000002	Phosphoribosylformylglycinamidine synthase
614	807	Gene3D	G3DSA:3.30.1330.10	-
614	807	InterPro	IPR036921	PurM-like, N-terminal domain superfamily
36	150	Pfam	PF18076	Formylglycinamide ribonucleotide amidotransferase N-terminal
36	150	InterPro	IPR040707	Phosphoribosylformylglycinamidine synthase, N-terminal
153	213	FunFam	G3DSA:1.10.8.750:FF:000002	Phosphoribosylformylglycinamidine synthase
214	420	Gene3D	G3DSA:3.30.1330.10	-
214	420	InterPro	IPR036921	PurM-like, N-terminal domain superfamily
421	606	FunFam	G3DSA:3.90.650.10:FF:000002	Phosphoribosylformylglycinamidine synthase
205	600	CDD	cd02203	PurL_repeat1
619	807	FunFam	G3DSA:3.30.1330.10:FF:000005	Phosphoribosylformylglycinamidine synthase
3	1293	PANTHER	PTHR10099	PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE
2	1295	Hamap	MF_00419	Phosphoribosylformylglycinamidine synthase [purL].
2	1295	InterPro	IPR010073	Phosphoribosylformylglycinamidine synthase PurL
432	588	Pfam	PF02769	AIR synthase related protein, C-terminal domain
432	588	InterPro	IPR010918	PurM-like, C-terminal domain
831	966	Pfam	PF02769	AIR synthase related protein, C-terminal domain
831	966	InterPro	IPR010918	PurM-like, C-terminal domain
981	1295	FunFam	G3DSA:3.40.50.880:FF:000008	Phosphoribosylformylglycinamidine synthase
981	1295	Gene3D	G3DSA:3.40.50.880	-
981	1295	InterPro	IPR029062	Class I glutamine amidotransferase-like
153	213	Gene3D	G3DSA:1.10.8.750	Phosphoribosylformylglycinamidine synthase, linker domain
172	220	Pfam	PF18072	Formylglycinamide ribonucleotide amidotransferase linker domain
172	220	InterPro	IPR041609	Phosphoribosylformylglycinamidine synthase, linker domain
618	816	SUPERFAMILY	SSF55326	PurM N-terminal domain-like
618	816	InterPro	IPR036921	PurM-like, N-terminal domain superfamily
1035	1293	SUPERFAMILY	SSF52317	Class I glutamine amidotransferase-like
1035	1293	InterPro	IPR029062	Class I glutamine amidotransferase-like
808	980	Gene3D	G3DSA:3.90.650.10	-
808	980	InterPro	IPR036676	PurM-like, C-terminal domain superfamily
421	606	Gene3D	G3DSA:3.90.650.10	-
421	606	InterPro	IPR036676	PurM-like, C-terminal domain superfamily
221	428	SUPERFAMILY	SSF55326	PurM N-terminal domain-like
221	428	InterPro	IPR036921	PurM-like, N-terminal domain superfamily
809	980	FunFam	G3DSA:3.90.650.10:FF:000005	Phosphoribosylformylglycinamidine synthase
1042	1295	ProSiteProfiles	PS51273	Glutamine amidotransferase type 1 domain profile.
818	1033	SUPERFAMILY	SSF56042	PurM C-terminal domain-like
818	1033	InterPro	IPR036676	PurM-like, C-terminal domain superfamily
1039	1292	Pfam	PF13507	CobB/CobQ-like glutamine amidotransferase domain
431	615	SUPERFAMILY	SSF56042	PurM C-terminal domain-like
431	615	InterPro	IPR036676	PurM-like, C-terminal 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.

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_A0A0H3GWU2	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00823	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
4				0.899
2				0.892
55				0.892
1				0.587

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	45.45	0.973
2	20.69	0.86
3	12.35	0.648
4	8.34	0.444
5	7.71	0.408

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
23				0.905
43				0.867
1				0.643
9				0.369

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	51.98	0.982
2	21.82	0.874
3	10.88	0.584
4	7.5	0.395
5	4.55	0.195

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
ACP	2HRY	Q9X0X3	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)…`
ANP	3UMM	P74881	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)…`
FGR	2HS3	Q9X0X3	314.2 Da LogP -3.60 TPSA 174.7	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@@H](O1)NC(=O)CNC=O)O)O)…`
XE	4MGH	P74881	131.3 Da LogP 0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Xe]`

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
ZINC12360002	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…`
ZINC12360703	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…`
ZINC12503599	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…`
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)(…`
ZINC31977053	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)…`
ZINC4806433	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…`
ZINC53683898	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(=…`
ZINC8586019	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)…`
ZINC8586020	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(=…`
ZINC8586021	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…`
ZINC8586022	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(=…`
ZINC13518964	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.741	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	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.741	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	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.741	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	0.741	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	0.741	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	0.729	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.726	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	0.726	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	0.726	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	0.726	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	0.712	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	0.712	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	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423	0.703	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC105469665	0.694	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	0.694	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	0.694	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	0.694	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	0.694	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	0.694	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	0.694	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	0.677	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	0.677	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	0.677	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	0.677	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	0.672	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…`
ZINC1582675	0.667	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486730	0.667	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486734	0.667	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`
ZINC5486740	0.667	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.