Protein profile

KP13_03032

UvrABC system protein B

Genome: KpKP13

Gene: uvrB AHE45582.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GKA2

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Amino acids 673

Annotations 11

Features 46

PDB binders 6

Druggability 0.333

Overview

Basic information about this protein and its source genome.

Accession: KP13_03032
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: uvrB AHE45582.1
Status: annotated
Amino acids: 673
Structure source: AlphaFold + ColabFold

GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. GO:0006289 A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts). GO:0005515 Binding to a protein. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0009380 Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 33.036
Human E-value: 6.44e-06
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 79.315
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 87.49

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 0.333

Structure A0A0H3GKA2

Pocket Pocket 43

P2Rank 0.91

Structure A0A0H3GKA2

Pocket Pocket 1

ColabFold model

FPocket 0.257 · Pocket 19

P2Rank 0.877 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 4106 / 4744 genomes with a hit

Normalized 0.866

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

11 GO

Gene Ontology (GO)

GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0006289 A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
GO:0005515 Binding to a protein.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0009380 Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0009381 Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid at sites flanking regions of damaged DNA to which the Uvr ABC excinuclease complexes bind.
GO:0004386 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
GO:0009432 An error-prone process for repairing damaged microbial DNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

46 records

Show feature table

Start	End	DB	Term	Name
231	414	FunFam	G3DSA:3.40.50.300:FF:000477	UvrABC system protein B
636	656	Coils	Coil	Coil
5	415	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
5	415	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
37	584	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
37	584	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
264	284	Coils	Coil	Coil
4	243	Gene3D	G3DSA:3.40.50.300	-
4	243	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
269	414	Gene3D	G3DSA:3.40.50.300	-
269	414	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
431	597	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
431	597	InterPro	IPR001650	Helicase, C-terminal
5	666	NCBIfam	TIGR00631	excinuclease ABC subunit UvrB
5	666	InterPro	IPR004807	UvrABC system, subunit B
26	183	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
26	183	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
9	425	SMART	SM00487	ultradead3
9	425	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
634	667	Pfam	PF02151	UvrB/uvrC motif
634	667	InterPro	IPR001943	UVR domain
3	668	Hamap	MF_00204	UvrABC system protein B [uvrB].
3	668	InterPro	IPR004807	UvrABC system, subunit B
441	544	Pfam	PF00271	Helicase conserved C-terminal domain
441	544	InterPro	IPR001650	Helicase, C-terminal
633	668	ProSiteProfiles	PS50151	UVR domain profile.
633	668	InterPro	IPR001943	UVR domain
613	673	Gene3D	G3DSA:4.10.860.10	UVR domain
625	669	SUPERFAMILY	SSF46600	C-terminal UvrC-binding domain of UvrB
625	669	InterPro	IPR036876	UVR domain superfamily
159	249	Pfam	PF17757	UvrB interaction domain
159	249	InterPro	IPR041471	UvrB, interaction domain
3	669	PANTHER	PTHR24029	UVRABC SYSTEM PROTEIN B
3	669	InterPro	IPR004807	UvrABC system, subunit B
415	590	FunFam	G3DSA:3.40.50.300:FF:000257	UvrABC system protein B
552	593	Pfam	PF12344	Ultra-violet resistance protein B
552	593	InterPro	IPR024759	UvrB, YAD/RRR-motif-containing domain
460	546	SMART	SM00490	helicmild6
460	546	InterPro	IPR001650	Helicase, C-terminal
16	92	Pfam	PF04851	Type III restriction enzyme, res subunit
16	92	InterPro	IPR006935	Helicase/UvrB, N-terminal
415	590	Gene3D	G3DSA:3.40.50.300	-
415	590	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
5	414	CDD	cd17916	DEXHc_UvrB
1	230	FunFam	G3DSA:3.40.50.300:FF:000401	UvrABC system protein B
420	590	CDD	cd18790	SF2_C_UvrB

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 + 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_A0A0H3GKA2	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_03032	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
43				0.333

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	21.99	0.876
2	10.06	0.542
3	4.67	0.203
4	2.38	0.063
5	1.72	0.03

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
19				0.257

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	19.58	0.841
2	8.64	0.462
3	7.53	0.396
4	7.26	0.378
5	5.16	0.238

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.

56 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
ANP	6L5N	Q9NR30	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	3PEW	P20449	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
FLQ	2FDC	P56981	516.6 Da LogP 4.09 TPSA 134.2	1 viol.	✓ Clean	`CC(=O)NCCCCCCNC(=O)c1ccc2c(c1)C3(c4ccc(cc4Oc5c3…`
FLU	2NMV	P37954	332.3 Da LogP 3.97 TPSA 87.7	✓ Ro5	✓ Clean	`c1ccc(c(c1)C2=C3C=CC(=O)C=C3Oc4c2ccc(c4)O)C(=O)O`
IHP	3RRN	P20449	660.0 Da LogP -3.13 TPSA 400.6	3 viol.	✓ Clean	`C1(C(C(C(C(C1OP(=O)(O)O)OP(=O)(O)O)OP(=O)(O)O)O…`
M2A	5ELX	P20449	560.4 Da LogP 0.16 TPSA 250.7	3 viol.	✓ Clean	`CNc1ccccc1C(=O)O[C@@H]2[C@@H]([C@@H](O[C@H]2n3c…`

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
ZINC3872582	1.000	332.3 Da LogP 3.97 TPSA 87.7	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1-c1c2ccc(=O)cc-2oc2cc(O)ccc12`
ZINC205587376	0.821	474.5 Da LogP 3.91 TPSA 131.1	✓ Ro5	✓ Clean	`NCCCCCCNC(=O)c1ccc2c(c1)C1(OC2=O)c2ccc(O)cc2Oc2…`
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(=…`
ZINC101257688	0.807	489.5 Da LogP 4.04 TPSA 142.4	✓ Ro5	✓ Clean	`O=C(O)CCCCCNC(=O)c1ccc2c(c1)C1(OC2=O)c2ccc(O)cc…`
ZINC5030658	0.771	376.3 Da LogP 3.67 TPSA 125.0	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2c3ccc(=O)cc-3oc3cc(O)ccc23)c(C(=…`
ZINC4344388	0.760	346.3 Da LogP 4.06 TPSA 76.7	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1-c1c2ccc(=O)cc-2oc2cc(O)ccc12`
ZINC4582277	0.756	304.3 Da LogP 3.98 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1ccc2c(-c3ccccc3O)c3ccc(O)cc3oc-2c1`
ZINC5248684	0.755	376.3 Da LogP 3.67 TPSA 125.0	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)O)c(-c2c3ccc(=O)cc-3oc3cc(O)cc…`
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…`
ZINC13556870	0.722	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)O[C@H]1[C@@H](O)[C@@H](O)[C@H](O)[C@@H…`
ZINC71789368	0.722	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)O[C@H]1[C@H](OP(=O)(O)O)[C@@H](O)[C@H]…`
ZINC71792243	0.722	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)O[C@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H…`
ZINC205997784	0.721	458.4 Da LogP 4.10 TPSA 153.9	✓ Ro5	Alert	`[N-]=[N+]=NCCCNC(=O)c1ccc2c(c1)C1(OC2=O)c2ccc(O…`
ZINC25762071	0.720	362.3 Da LogP 3.13 TPSA 139.8	✓ Ro5	✓ Clean	`Nc1cc(C(=O)O)c(-c2c3ccc(=O)cc-3oc3cc(O)ccc23)cc…`
ZINC4344383	0.717	288.3 Da LogP 4.27 TPSA 50.4	✓ Ro5	✓ Clean	`O=c1ccc2c(-c3ccccc3)c3ccc(O)cc3oc-2c1`
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](…`
ZINC953075800	0.712	474.5 Da LogP 3.91 TPSA 131.1	✓ Ro5	✓ Clean	`NCCCCCCNC(=O)c1ccc2c(c1)C(=O)OC21c2ccc(O)cc2Oc2…`
ZINC230495868	0.707	413.4 Da LogP 3.03 TPSA 105.1	✓ Ro5	✓ Clean	`C#CCNC(=O)c1ccc2c(c1)C1(OC2=O)c2ccc(O)cc2Oc2cc(…`
ZINC100015959	0.706	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)O[C@H]1[C@H](O)[C@@H](OP(=O)(O)O)[C@H]…`
ZINC1501016356	0.706	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)OC1C(O)[C@H](OP(=O)(O)O)C(O)[C@H](OP(=…`

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.