Protein profile

PA4922

azurin

Genome: NC_002516.2

Gene: azu PA4922 Structure source: Experimental + AlphaFold UniProt P00282

Export view

Amino acids 148

Annotations 7

Features 20

PDB binders 9

Druggability 0.699

Overview

Basic information about this protein and its source genome.

Accession: PA4922
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: azu PA4922
Status: annotated
Amino acids: 148
Structure source: Experimental + AlphaFold

GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). 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:0005507 Binding to a copper (Cu) ion. GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways. GO:0042802 Binding to an identical protein or proteins. GO:0046914 Binding to a transition metal ions; a transition metal is an element whose atom has an incomplete d-subshell of extranuclear electrons, or which gives rise to a cation or cations with an incomplete d-subshell. Transition metals often have more than one valency state. Biologically relevant transition metals include vanadium, manganese, iron, copper, cobalt, nickel, molybdenum and silver.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Periplasmic

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 0.699

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MLRKLAAVSLLSLLSAPLLAAECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTFPGHSALMKGTLTLK

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
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:0005507 Binding to a copper (Cu) ion.
GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
GO:0042802 Binding to an identical protein or proteins.
GO:0046914 Binding to a transition metal ions; a transition metal is an element whose atom has an incomplete d-subshell of extranuclear electrons, or which gives rise to a cation or cations with an incomplete d-subshell. Transition metals often have more than one valency state. Biologically relevant transition metals include vanadium, manganese, iron, copper, cobalt, nickel, molybdenum and silver.
GO:0008270 Binding to a zinc ion (Zn).

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
23	147	NCBIfam	TIGR02695	azurin
23	147	InterPro	IPR014068	Azurin
21	147	SUPERFAMILY	SSF49503	Cupredoxins
21	147	InterPro	IPR008972	Cupredoxin
1	20	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
16	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
21	148	Pfam	PF00127	Copper binding proteins, plastocyanin/azurin family
21	148	InterPro	IPR000923	Blue (type 1) copper domain
5	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
21	148	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
21	148	PANTHER	PTHR38439	AURACYANIN-B
23	147	CDD	cd13922	Azurin
1	20	SignalP_EUK	SignalP-noTM	SignalP-noTM
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
125	141	ProSitePatterns	PS00196	Type-1 copper (blue) proteins signature.
125	141	InterPro	IPR028871	Blue (type 1) copper protein, binding site
21	148	Gene3D	G3DSA:2.60.40.420	-
21	148	InterPro	IPR008972	Cupredoxin
21	148	FunFam	G3DSA:2.60.40.420:FF:000040	Azurin
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region

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...

Legend High Medium Low

Structural evidence

111 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 8F5L	X-ray	1.15 Å	A,B	100.0% 1-148	PDBe RCSB PDBj File	Viewing
PDB 8F5K	X-ray	1.25 Å	A,B,C,D	100.0% 1-148	PDBe RCSB PDBj File	Loaded
PDB 1AG0	X-ray	2.40 Å	A,B	87.2% 20-148	PDBe RCSB PDBj File	Loaded
PDB 3FSA	X-ray	0.98 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3FS9	X-ray	1.05 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2FT6	X-ray	1.25 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2I7S	X-ray	1.35 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3N2J	X-ray	1.35 Å	A,B,C,D,E,F,G,H,I,J,K,L	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1JZG	X-ray	1.40 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2FNW	X-ray	1.40 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2FT7	X-ray	1.40 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3IBO	X-ray	1.45 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 7TC5	X-ray	1.45 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4KOC	X-ray	1.46 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 7TNC	X-ray	1.47 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4BWW	X-ray	1.48 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1JZF	X-ray	1.50 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1XB3	X-ray	1.50 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2I7O	X-ray	1.50 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4JKN	X-ray	1.54 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4MFH	X-ray	1.54 Å	A,B,C	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2FT8	X-ray	1.55 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2HX7	X-ray	1.55 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1JZE	X-ray	1.60 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2GHZ	X-ray	1.60 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2HX8	X-ray	1.60 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2XV0	X-ray	1.60 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2XV2	X-ray	1.60 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4HHG	X-ray	1.60 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 6GYI	X-ray	1.60 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2FTA	X-ray	1.61 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1JZI	X-ray	1.62 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4QKT	X-ray	1.64 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1CC3	X-ray	1.65 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1JZH	X-ray	1.70 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2GI0	X-ray	1.70 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2HX9	X-ray	1.70 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3UGE	X-ray	1.70 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4K9J	X-ray	1.70 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4KO6	X-ray	1.74 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4KO5	X-ray	1.79 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1GR7	X-ray	1.80 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1I53	X-ray	1.80 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1JZJ	X-ray	1.80 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3FT0	X-ray	1.80 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3JTB	X-ray	1.80 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1XB6	X-ray	1.82 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1E65	X-ray	1.85 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4KOB	X-ray	1.87 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 5I26	X-ray	1.89 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1R1C	X-ray	1.90 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1VLX	X-ray	1.90 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2AZU	X-ray	1.90 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3FQ1	X-ray	1.90 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3FQY	X-ray	1.90 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4AZU	X-ray	1.90 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4HIP	X-ray	1.90 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 5AZU	X-ray	1.90 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3FQ2	X-ray	1.91 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4WKX	X-ray	1.94 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 5I28	X-ray	1.95 Å	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1E5Y	X-ray	2.00 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1E5Z	X-ray	2.00 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1EZL	X-ray	2.00 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1JVL	X-ray	2.00 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1XB8	X-ray	2.00 Å	A,C	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3FSW	X-ray	2.00 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3FSZ	X-ray	2.00 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4HHW	X-ray	2.00 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4QLW	X-ray	2.00 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 9OH7	X-ray	2.00 Å	A,B,E,G	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 9OH6	X-ray	2.04 Å	B,E,H,K	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4KO9	X-ray	2.05 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4KO7	X-ray	2.07 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3AZU	X-ray	2.10 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3FPY	X-ray	2.10 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3JT2	X-ray	2.10 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3NP3	X-ray	2.10 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1E67	X-ray	2.14 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1ILS	X-ray	2.20 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1NZR	X-ray	2.20 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2TSA	X-ray	2.20 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 4HZ1	X-ray	2.20 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 7U2F	X-ray	2.20 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2HXA	X-ray	2.21 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2IDF	X-ray	2.25 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3NP4	X-ray	2.25 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1BEX	X-ray	2.30 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1ETJ	X-ray	2.30 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1ILU	X-ray	2.30 Å	A,B,C,D,E,F,G,H,I,K,L,M	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2OJ1	X-ray	2.30 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2TSB	X-ray	2.30 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2XV3	X-ray	2.30 Å	A,B	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3FSV	X-ray	2.30 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3IN0	X-ray	2.35 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1AZR	X-ray	2.40 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3OQR	X-ray	2.40 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1AZN	X-ray	2.60 Å	A,B,C,D	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3IN2	X-ray	2.60 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1AZU	X-ray	2.70 Å	A	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 1JVO	X-ray	2.75 Å	A,B,C,D,E,F,G,H,I,J,K,L	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 2IWE	X-ray	2.83 Å	A,D,G,J	86.5% 21-148	PDBe RCSB PDBj File	Loaded
PDB 3U25	X-ray	1.18 Å	A,B	85.8% 22-148	PDBe RCSB PDBj File	Loaded
PDB 6MJS	X-ray	1.85 Å	A,B,C,D	85.8% 22-148	PDBe RCSB PDBj File	Loaded
PDB 7TC6	X-ray	1.85 Å	A,B	85.8% 22-148	PDBe RCSB PDBj File	Loaded
PDB 6MJT	X-ray	1.89 Å	A,B	85.8% 22-148	PDBe RCSB PDBj File	Loaded
PDB 6IAV	X-ray	2.00 Å	A,B,C,D	85.8% 22-148	PDBe RCSB PDBj File	Loaded
PDB 6MJR	X-ray	2.01 Å	A,B,C,D	85.8% 22-148	PDBe RCSB PDBj File	Loaded
PDB 7YGI	X-ray	2.10 Å	C,D	83.1% 23-145	PDBe RCSB PDBj File	Loaded
PDB 5YT7	X-ray	1.66 Å	A,B,C,D	77.0% 21-134	PDBe RCSB PDBj File	Loaded
PDB 5SYD	X-ray	2.40 Å	A,B	58.1% 63-148	PDBe RCSB PDBj File	Loaded
AlphaFold PA4922	AlphaFold	—	—	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
2				0.725
3				0.269

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.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
144	1JVL 2.00 Å Open crystal	122.1 Da LogP -1.72 TPSA 60.7	✓ Ro5	✓ Clean	`C[N+](CO)(CO)CO`
2IH	2IWE 2.83 Å Open crystal	218.3 Da LogP 2.34 TPSA 35.6	✓ Ro5	✓ Clean	`c1cn(cn1)CCCCCCn2ccnc2`
AZI	2TSB 2.30 Å Open crystal	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
DPT	1I53 1.80 Å Open crystal	208.3 Da LogP 3.40 TPSA 25.8	✓ Ro5	✓ Clean	`Cc1ccnc2c1ccc3c2nccc3C`
OPP	1JVL 2.00 Å Open crystal	236.2 Da LogP -1.23 TPSA 84.0	✓ Ro5	✓ Clean	`C1=CC(=O)N(C1=O)COCN2C(=O)C=CC2=O`
REP	1JZI 1.62 Å Open crystal	—	—	—	`C1=C[N]2=C3C(=C1)C=CC4=CC=C[N](=C43)[Re]2(C#O)(…`
REQ	2I7O 1.50 Å Open crystal	—	—	—	`CC1=C2C=CC3=C4C2=[N](C=C1)[Re]([N]4=CC=C3C)(C#O…`
RTA	1JZH 1.70 Å Open crystal	513.7 Da LogP 3.71 TPSA 16.2	1 viol.	✓ Clean	`C1CCN2C(C1)C3CCCC4N3[Ru+2]25(N6C4CCCC6)N7CCCCC7…`
RTC	1I53 1.80 Å Open crystal	—	—	—	`C(#O)[Re+](C#O)C#O`

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.

No PDB ligands found through similar proteins.

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
ZINC120461	1.000	208.3 Da LogP 3.40 TPSA 25.8	✓ Ro5	✓ Clean	`Cc1ccnc2c1ccc1c(C)ccnc12`
ZINC2384689	1.000	236.2 Da LogP -1.23 TPSA 84.0	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1COCN1C(=O)C=CC1=O`
ZINC100012649	0.792	236.4 Da LogP 4.80 TPSA 17.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCn1ccnc1`
ZINC43300577	0.792	208.3 Da LogP 4.02 TPSA 17.8	✓ Ro5	✓ Clean	`CCCCCCCCCCn1ccnc1`
ZINC44069494	0.792	224.3 Da LogP 3.00 TPSA 38.0	✓ Ro5	✓ Clean	`OCCCCCCCCCCn1ccnc1`
ZINC71773476	0.792	254.4 Da LogP 4.32 TPSA 17.8	✓ Ro5	✓ Clean	`SCCCCCCCCCCCn1ccnc1`
ZINC38337192	0.704	210.3 Da LogP 2.31 TPSA 55.1	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCn1ccnc1`
ZINC207622875	0.692	222.3 Da LogP 3.71 TPSA 25.8	✓ Ro5	✓ Clean	`Cc1cc(C)c2ccc3c(C)ccnc3c2n1`
ZINC68755424	0.654	212.1 Da LogP 3.85 TPSA 12.9	✓ Ro5	✓ Clean	`Cc1ccnc2c(Cl)c(Cl)ccc12`
ZINC85399522	0.607	240.1 Da LogP 3.44 TPSA 12.9	✓ Ro5	✓ Clean	`Cc1ccnc2c(Br)c(F)ccc12`
ZINC85399528	0.607	287.1 Da LogP 3.29 TPSA 12.9	✓ Ro5	✓ Clean	`Cc1ccnc2c(I)c(F)ccc12`
ZINC122411683	0.600	200.3 Da LogP 2.91 TPSA 17.8	✓ Ro5	✓ Clean	`c1ccc(CCCCn2ccnc2)cc1`
ZINC13230214	0.594	244.3 Da LogP 3.52 TPSA 27.1	✓ Ro5	✓ Clean	`c1ccc(OCCCCCCn2ccnc2)cc1`
ZINC40571760	0.593	222.1 Da LogP 3.31 TPSA 12.9	✓ Ro5	✓ Clean	`Cc1ccnc2c(Br)cccc12`
ZINC77273545	0.591	264.2 Da LogP -1.15 TPSA 84.0	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCN1C(=O)C=CC1=O`
ZINC4203455	0.579	220.2 Da LogP -1.16 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCN1C(=O)C=CC1=O`
ZINC165715	0.567	203.3 Da LogP 2.39 TPSA 22.8	✓ Ro5	✓ Clean	`Cc1ccc(C)n1CCCn1ccnc1`
ZINC145341967	0.565	440.4 Da LogP -1.08 TPSA 120.9	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC1857792026	0.565	484.5 Da LogP -1.06 TPSA 130.1	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2387138	0.565	352.3 Da LogP -1.11 TPSA 102.4	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC2572930	0.565	308.3 Da LogP -1.13 TPSA 93.2	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCN1C(=O)C=CC1=O`
ZINC5372881	0.565	396.4 Da LogP -1.10 TPSA 111.7	✓ Ro5	✓ Clean	`O=C1C=CC(=O)N1CCOCCOCCOCCOCCN1C(=O)C=CC1=O`
ZINC113769704	0.563	279.2 Da LogP 3.67 TPSA 17.8	✓ Ro5	✓ Clean	`Brc1ccc(CCCCn2ccnc2)cc1`
ZINC2493375	0.563	216.3 Da LogP 2.74 TPSA 27.1	✓ Ro5	✓ Clean	`c1ccc(OCCCCn2ccnc2)cc1`
ZINC13284757	0.559	260.3 Da LogP 3.14 TPSA 36.3	✓ Ro5	✓ Clean	`COc1ccc(OCCCCCn2ccnc2)cc1`
ZINC23115344	0.559	274.4 Da LogP 3.53 TPSA 36.3	✓ Ro5	✓ Clean	`COc1ccc(OCCCCCCn2ccnc2)cc1`
ZINC23115438	0.559	264.8 Da LogP 3.79 TPSA 27.1	✓ Ro5	✓ Clean	`Clc1ccc(OCCCCCn2ccnc2)cc1`
ZINC2386332997	0.559	266.4 Da LogP 3.57 TPSA 44.1	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)CCCCCCCn1ccnc1`
ZINC2497081	0.559	278.8 Da LogP 4.18 TPSA 27.1	✓ Ro5	✓ Clean	`Clc1ccc(OCCCCCCn2ccnc2)cc1`
ZINC2497219	0.559	309.2 Da LogP 3.89 TPSA 27.1	✓ Ro5	✓ Clean	`Brc1ccc(OCCCCCn2ccnc2)cc1`
ZINC2895689	0.559	272.4 Da LogP 4.14 TPSA 27.1	✓ Ro5	✓ Clean	`Cc1cc(C)cc(OCCCCCCn2ccnc2)c1`
ZINC2901107	0.559	248.3 Da LogP 3.27 TPSA 27.1	✓ Ro5	✓ Clean	`Fc1ccc(OCCCCCn2ccnc2)cc1`
ZINC6110405	0.559	323.2 Da LogP 4.29 TPSA 27.1	✓ Ro5	✓ Clean	`Brc1ccc(OCCCCCCn2ccnc2)cc1`
ZINC5387101	0.548	203.3 Da LogP -0.18 TPSA 64.0	✓ Ro5	✓ Clean	`CS(=O)(=O)NCCCn1ccnc1`
ZINC1794320	0.545	270.5 Da LogP 1.76 TPSA 46.9	✓ Ro5	✓ Clean	`O=C(NCCCn1ccnc1)C(Cl)(Cl)Cl`
ZINC27898231	0.545	269.3 Da LogP 1.96 TPSA 55.2	✓ Ro5	✓ Clean	`O=C1c2ccccc2C(=O)N1CCCCn1ccnc1`
ZINC32628619	0.545	219.2 Da LogP 0.73 TPSA 64.7	✓ Ro5	✓ Clean	`O=C(NCCCn1ccnc1)n1ccnc1`
ZINC13284753	0.543	272.4 Da LogP 4.14 TPSA 27.1	✓ Ro5	✓ Clean	`Cc1cccc(C)c1OCCCCCCn1ccnc1`
ZINC13284776	0.543	264.8 Da LogP 3.79 TPSA 27.1	✓ Ro5	✓ Clean	`Clc1ccccc1OCCCCCn1ccnc1`
ZINC23115383	0.543	262.3 Da LogP 3.66 TPSA 27.1	✓ Ro5	✓ Clean	`Fc1ccccc1OCCCCCCn1ccnc1`
ZINC23115408	0.543	258.4 Da LogP 3.75 TPSA 27.1	✓ Ro5	✓ Clean	`Cc1cccc(C)c1OCCCCCn1ccnc1`
ZINC23115544	0.543	260.3 Da LogP 3.14 TPSA 36.3	✓ Ro5	✓ Clean	`COc1ccccc1OCCCCCn1ccnc1`
ZINC2494225	0.543	309.2 Da LogP 3.89 TPSA 27.1	✓ Ro5	✓ Clean	`Brc1ccccc1OCCCCCn1ccnc1`
ZINC2497234	0.543	323.2 Da LogP 4.29 TPSA 27.1	✓ Ro5	✓ Clean	`Brc1ccccc1OCCCCCCn1ccnc1`
ZINC2842687	0.543	258.4 Da LogP 3.83 TPSA 27.1	✓ Ro5	✓ Clean	`Cc1ccccc1OCCCCCCn1ccnc1`
ZINC2899537	0.543	272.4 Da LogP 4.06 TPSA 27.1	✓ Ro5	✓ Clean	`Cc1cc(C)c(OCCCCCn2ccnc2)c(C)c1`
ZINC3106111	0.543	274.4 Da LogP 3.53 TPSA 36.3	✓ Ro5	✓ Clean	`COc1ccccc1OCCCCCCn1ccnc1`
ZINC3876762	0.543	286.4 Da LogP 4.45 TPSA 27.1	✓ Ro5	✓ Clean	`Cc1cc(C)c(OCCCCCCn2ccnc2)c(C)c1`
ZINC5387551	0.543	248.3 Da LogP 3.27 TPSA 27.1	✓ Ro5	✓ Clean	`Fc1ccccc1OCCCCCn1ccnc1`
ZINC196903237	0.536	283.1 Da LogP 3.46 TPSA 12.9	✓ Ro5	✓ Clean	`Cc1ccnc2c(C)cc(I)cc12`

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.