Protein profile

PA4034

aquaporin Z

Genome: NC_002516.2

Gene: PA4034 aqpZ Structure source: AlphaFold UniProt Q9HWZ3

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Amino acids 229

Annotations 6

Features 51

PDB binders 2

Druggability 0.499

Overview

Basic information about this protein and its source genome.

Accession: PA4034
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4034 aqpZ
Status: annotated
Amino acids: 229
Structure source: AlphaFold

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:0015250 Enables the energy-independent facilitated diffusion of water through a transmembrane aqueous pore or channel. GO:0006833 The directed movement of water (H2O) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0015267 Enables the energy-independent facilitated diffusion of a solute through a transmembrane aqueous pore or channel. Stereospecificity is not exhibited but this transport may be specific for a particular molecular species or class of molecules.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 44.262
Human E-value: 1.91e-09
Gut microbiome off-target: hit
Essential (DEG): N
Localization: CytoplasmicMembrane

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 0.499

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

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:0015250 Enables the energy-independent facilitated diffusion of water through a transmembrane aqueous pore or channel.
GO:0006833 The directed movement of water (H2O) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0015267 Enables the energy-independent facilitated diffusion of a solute through a transmembrane aqueous pore or channel. Stereospecificity is not exhibited but this transport may be specific for a particular molecular species or class of molecules.

Sequence Features

Domain/signature hits from InterPro and related databases.

51 records

Show feature table

Start	End	DB	Term	Name
1	7	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
80	102	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
129	151	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
60	68	ProSitePatterns	PS00221	MIP family signature.
60	68	InterPro	IPR022357	Major intrinsic protein, conserved site
1	226	Gene3D	G3DSA:1.20.1080.10	Glycerol uptake facilitator protein.
1	226	InterPro	IPR023271	Aquaporin-like
204	224	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	19	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
6	221	NCBIfam	TIGR00861	MIP family channel protein
6	221	InterPro	IPR000425	Major intrinsic protein
1	225	SUPERFAMILY	SSF81338	Aquaporin-like
1	225	InterPro	IPR023271	Aquaporin-like
159	178	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
8	19	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
1	25	Phobius	SIGNAL_PEPTIDE	Signal peptide region
103	126	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
80	102	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
26	34	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
3	225	PANTHER	PTHR19139	AQUAPORIN TRANSPORTER
3	225	InterPro	IPR034294	Aquaporin transporter
1	228	Hamap	MF_01146	Aquaporin Z [aqpZ].
1	228	InterPro	IPR023743	Aquaporin Z
35	59	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
60	79	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
225	229	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1	229	FunFam	G3DSA:1.20.1080.10:FF:000007	Aquaporin Z
148	158	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
127	147	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
20	25	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
158	180	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
179	203	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
5	27	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
37	59	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
2	224	CDD	cd00333	MIP
2	224	InterPro	IPR000425	Major intrinsic protein
203	225	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
165	187	PRINTS	PR00783	Major intrinsic protein family signature
165	187	InterPro	IPR000425	Major intrinsic protein
42	66	PRINTS	PR00783	Major intrinsic protein family signature
42	66	InterPro	IPR000425	Major intrinsic protein
2	21	PRINTS	PR00783	Major intrinsic protein family signature
2	21	InterPro	IPR000425	Major intrinsic protein
79	98	PRINTS	PR00783	Major intrinsic protein family signature
79	98	InterPro	IPR000425	Major intrinsic protein
135	153	PRINTS	PR00783	Major intrinsic protein family signature
135	153	InterPro	IPR000425	Major intrinsic protein
204	224	PRINTS	PR00783	Major intrinsic protein family signature
204	224	InterPro	IPR000425	Major intrinsic protein
2	221	Pfam	PF00230	Major intrinsic protein
2	221	InterPro	IPR000425	Major intrinsic protein

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 PA4034	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
3				0.497
1				0.222

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.

63 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
3PE	3M9I	Q6J8I9	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
PS6	3D9S	P55064	567.7 Da LogP 5.27 TPSA 171.7	2 viol.	✓ Clean	`CCCCCCCCCCCCCC(=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
AZM	P55088	—	222.3 Da LogP -0.86 TPSA 115.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(s1)S(=O)(=O)N`
CHEMBL121	P41181	—	357.4 Da LogP 2.49 TPSA 71.5	✓ Ro5	✓ Clean	`CN(CCOc1ccc(CC2SC(=O)NC2=O)cc1)c1ccccn1`
CHEMBL128	P55088	—	295.4 Da LogP 1.32 TPSA 65.2	✓ Ro5	✓ Clean	`CNS(=O)(=O)Cc1ccc2[nH]cc(CCN(C)C)c2c1`
CHEMBL16	P55088	—	252.3 Da LogP 1.77 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)C(c2ccccc2)(c2ccccc2)N1`
CHEMBL536151	P55087	—	383.7 Da LogP 5.34 TPSA 49.3	1 viol.	✓ Clean	`O=C(Nc1cc(C(F)(F)F)cc(C(F)(F)F)c1)c1cc(Cl)ccc1O`
CHEMBL687	P55088	—	214.2 Da LogP 0.29 TPSA 89.3	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(S(N)(=O)=O)cc1`
CHEMBL741	P55088	—	256.1 Da LogP 2.01 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1nnc(-c2cccc(Cl)c2Cl)c(N)n1`
EZL	P55088	—	258.3 Da LogP 1.34 TPSA 82.3	✓ Ro5	✓ Clean	`CCOc1ccc2c(c1)sc(n2)S(=O)(=O)N`
FOK	P41181	—	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`CC(=O)O[C@H]1[C@H]([C@H]2C(CC[C@@H]([C@@]2([C@@…`
TOR	P55088	—	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(O[C@@H]2CO[C@@]3([C@H]([C@@H]2O1)OC(O3)(C)C…`
ZON	P55087	—	212.2 Da LogP 0.62 TPSA 86.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(no2)CS(=O)(=O)N`

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
ZINC102190506	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC13156	1.000	256.1 Da LogP 2.01 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1nnc(-c2cccc(Cl)c2Cl)c(N)n1`
ZINC134036	1.000	214.2 Da LogP 0.29 TPSA 89.3	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(S(N)(=O)=O)cc1`
ZINC13612334	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2CO[C@]3(COS(N)(=O)=O)OC(C)(C)O[C@@…`
ZINC13783471	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@H](OC(C)…`
ZINC13783493	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2CO[C@]3(COS(N)(=O)=O)OC(C)(C)O[C@…`
ZINC14360	1.000	295.4 Da LogP 1.32 TPSA 65.2	✓ Ro5	✓ Clean	`CNS(=O)(=O)Cc1ccc2[nH]cc(CCN(C)C)c2c1`
ZINC144827766	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@@](C)(O1)[C@@H](O…`
ZINC1543366	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2CO[C@@]3(COS(N)(=O)=O)OC(C)(C)O[C@…`
ZINC23586802	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2CO[C@@]3(COS(N)(=O)=O)OC(C)(C)O[C@…`
ZINC248102933	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@@]2(O)[C@]3(C)[C@@H](O)CCC(…`
ZINC248102936	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@@]2(O)[C@]3(C)[C@H](O)CCC(C…`
ZINC2510358	1.000	252.3 Da LogP 1.77 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)C(c2ccccc2)(c2ccccc2)N1`
ZINC36385190	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@H](OC(C)…`
ZINC3813042	1.000	222.3 Da LogP -0.86 TPSA 115.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC3831557	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2CO[C@@]3(COS(N)(=O)=O)OC(C)(C)O[C…`
ZINC3831559	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2CO[C@]3(COS(N)(=O)=O)OC(C)(C)O[C@…`
ZINC3872620	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@H](OC(…`
ZINC3872621	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](OC…`
ZINC3872622	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@H](OC(…`
ZINC3872623	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](OC…`
ZINC3977779	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](OC…`
ZINC4321	1.000	212.2 Da LogP 0.62 TPSA 86.2	✓ Ro5	✓ Clean	`NS(=O)(=O)Cc1noc2ccccc12`
ZINC43574047	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2[C@@H]3OC(C)(C)O[C@@]3(COS(N)(=O)…`
ZINC4544736	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@]1(C)CC(=O)[C@]2(O)[C@@](C)(O1)[C@H](OC(C…`
ZINC56721	1.000	258.3 Da LogP 1.34 TPSA 82.3	✓ Ro5	✓ Clean	`CCOc1ccc2nc(S(N)(=O)=O)sc2c1`
ZINC56863626	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2[C@@H](CO[C@]3(COS(N)(=O)=O)OC(C)(…`
ZINC71789673	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@@H](OC(…`
ZINC71789674	1.000	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@@H](OC(…`
ZINC95616603	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2CO[C@@]3(COS(N)(=O)=O)OC(C)(C)O[C…`
ZINC96085732	1.000	339.4 Da LogP -0.40 TPSA 115.5	✓ Ro5	✓ Clean	`CC1(C)O[C@@H]2[C@@H]3OC(C)(C)O[C@]3(COS(N)(=O)=…`
ZINC968328	1.000	357.4 Da LogP 2.49 TPSA 71.5	✓ Ro5	✓ Clean	`CN(CCOc1ccc(C[C@@H]2SC(=O)NC2=O)cc1)c1ccccn1`
ZINC968330	1.000	357.4 Da LogP 2.49 TPSA 71.5	✓ Ro5	✓ Clean	`CN(CCOc1ccc(C[C@H]2SC(=O)NC2=O)cc1)c1ccccn1`
ZINC27416437	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC12970899	0.889	290.3 Da LogP 1.96 TPSA 89.3	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(-c2ccc(S(N)(=O)=O)cc2)cc1`
ZINC2382316250	0.887	452.5 Da LogP 2.09 TPSA 119.4	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@@H](OC(…`
ZINC27553862	0.887	452.5 Da LogP 2.09 TPSA 119.4	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](OC…`
ZINC13111092	0.852	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](O)…`
ZINC2069563917	0.852	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@]2(O)[C@](C)(O1)[C@@H](O)[…`
ZINC71766833	0.852	410.5 Da LogP 1.52 TPSA 113.3	✓ Ro5	✓ Clean	`C=C[C@@]1(C)CC(=O)[C@@]2(O)[C@](C)(O1)[C@@H](O)…`
ZINC6116337	0.815	270.3 Da LogP 1.91 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@](c2ccccc2)(c2ccc(F)cc2)N1`
ZINC6116537	0.815	270.3 Da LogP 1.91 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@](c2ccccc2)(c2ccc(F)cc2)N1`
ZINC2165131	0.800	369.4 Da LogP 1.09 TPSA 135.4	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(S(=O)(=O)Nc2ccc(S(N)(=O)=O)cc2)cc1`
ZINC242063	0.800	333.4 Da LogP 1.54 TPSA 118.4	✓ Ro5	✓ Clean	`CC(=O)Nc1ccc(C(=O)Nc2ccc(S(N)(=O)=O)cc2)cc1`
ZINC114897182	0.788	495.7 Da LogP 3.50 TPSA 84.2	✓ Ro5	Alert	`CNS(=O)(=O)Cc1ccc2[nH]c(Cc3ccc4[nH]cc(CCN(C)C)c…`
ZINC22061272	0.787	355.4 Da LogP -1.42 TPSA 135.8	✓ Ro5	✓ Clean	`CC1(C)O[C@H]2[C@@H]3O[C@](C)(CO)O[C@@H]3CO[C@@]…`
ZINC119642	0.786	268.3 Da LogP 1.48 TPSA 78.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@](c2ccccc2)(c2ccc(O)cc2)N1`
ZINC2048546	0.786	286.7 Da LogP 2.42 TPSA 58.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@](c2ccccc2)(c2ccc(Cl)cc2)N1`

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.