Protein profile

PA0767

elongation factor 4

Genome: NC_002516.2

Gene: le lepA PA0767 Structure source: AlphaFold UniProt Q9I5G8

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Amino acids 599

Annotations 8

Features 51

PDB binders 8

Druggability 0.856

Overview

Basic information about this protein and its source genome.

Accession: PA0767
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: le lepA PA0767
Status: annotated
Amino acids: 599
Structure source: AlphaFold

3.6.5.n1

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:0005525 Binding to GTP, guanosine triphosphate. GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. GO:0097216 Binding to guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions. GO:0043022 Binding to a ribosome. GO:0003746 Functions in chain elongation during polypeptide synthesis at the ribosome.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 52.83
Human E-value: 1.24e-10
Gut microbiome off-target: hit
Essential (DEG): Y
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 0.856

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

3.6.5.n1

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:0005525 Binding to GTP, guanosine triphosphate.
GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
GO:0097216 Binding to guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions.
GO:0043022 Binding to a ribosome.
GO:0003746 Functions in chain elongation during polypeptide synthesis at the ribosome.
GO:0045727 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

51 records

Show feature table

Start	End	DB	Term	Name
4	597	PANTHER	PTHR43512	TRANSLATION FACTOR GUF1-RELATED
4	597	InterPro	IPR006297	Elongation factor 4
4	188	FunFam	G3DSA:3.40.50.300:FF:000078	Elongation factor 4
8	186	CDD	cd01890	LepA
289	370	FunFam	G3DSA:3.30.70.870:FF:000004	Translation factor GUF1, mitochondrial
482	556	Gene3D	G3DSA:3.30.70.2570	-
482	556	InterPro	IPR038363	LepA, C-terminal domain superfamily
93	104	PRINTS	PR00315	GTP-binding elongation factor signature
93	104	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
129	138	PRINTS	PR00315	GTP-binding elongation factor signature
129	138	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
77	87	PRINTS	PR00315	GTP-binding elongation factor signature
77	87	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
9	22	PRINTS	PR00315	GTP-binding elongation factor signature
9	22	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
52	60	PRINTS	PR00315	GTP-binding elongation factor signature
52	60	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
5	187	ProSiteProfiles	PS51722	Translational (tr)-type guanine nucleotide-binding (G) domain profile.
5	187	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
295	373	SUPERFAMILY	SSF54980	EF-G C-terminal domain-like
295	373	InterPro	IPR035647	EF-G domain III/V-like
1	235	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
1	235	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
5	188	Gene3D	G3DSA:3.40.50.300	-
5	188	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
371	480	Gene3D	G3DSA:3.30.70.240	-
402	487	Pfam	PF00679	Elongation factor G C-terminus
402	487	InterPro	IPR000640	Elongation factor EFG, domain V-like
403	496	SUPERFAMILY	SSF54980	EF-G C-terminal domain-like
403	496	InterPro	IPR035647	EF-G domain III/V-like
208	278	Pfam	PF03144	Elongation factor Tu domain 2
208	278	InterPro	IPR004161	Translation elongation factor EFTu-like, domain 2
189	287	FunFam	G3DSA:2.40.30.10:FF:000015	Translation factor GUF1, mitochondrial
289	370	Gene3D	G3DSA:3.30.70.870	Elongation Factor G (Translational Gtpase), domain 3
482	556	FunFam	G3DSA:3.30.70.2570:FF:000001	Translation factor GUF1, mitochondrial
6	184	Pfam	PF00009	Elongation factor Tu GTP binding domain
6	184	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
189	288	Gene3D	G3DSA:2.40.30.10	Translation factors
490	596	Pfam	PF06421	GTP-binding protein LepA C-terminus
490	596	InterPro	IPR013842	GTP-binding protein LepA, C-terminal
1	599	Hamap	MF_00071	Elongation factor 4 [lepA].
1	599	InterPro	IPR006297	Elongation factor 4
371	480	FunFam	G3DSA:3.30.70.240:FF:000007	Translation factor GUF1, mitochondrial
194	279	CDD	cd03699	EF4_II
296	371	CDD	cd16260	EF4_III
9	175	NCBIfam	TIGR00231	small GTP-binding protein domain
9	175	InterPro	IPR005225	Small GTP-binding protein domain
404	482	CDD	cd03709	lepA_C
404	482	InterPro	IPR035654	Elongation factor 4, domain IV
6	598	NCBIfam	TIGR01393	translation elongation factor 4
6	598	InterPro	IPR006297	Elongation factor 4

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 PA0767	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
5				0.856
9				0.274

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.

58 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
5MU	5J8B	Q5SKA7	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
APR	1U2R	P32324	559.3 Da LogP -3.28 TPSA 291.5	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
G4P	4ZCM	P0A3B2	603.2 Da LogP -2.22 TPSA 345.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GCP	5A9W	P0A3B2	521.2 Da LogP -2.22 TPSA 289.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GNP	2YWF	O67618	522.2 Da LogP -2.76 TPSA 301.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
MOU	2NPF	P32324	690.8 Da LogP 4.50 TPSA 175.1	1 viol.	✓ Clean	`C[C@@H]1CC[C@@H]2[C@@H]1C[C@@]3([C@@H]4C[C@]2([…`
SO1	1N0U	P32324	494.6 Da LogP 2.49 TPSA 122.5	✓ Ro5	✓ Clean	`C[C@@H]1CC[C@@H]2[C@@H]1C[C@@]3([C@H]4CC([C@@]3…`
SOD	2E1R	P32324	519.1 Da LogP 4.85 TPSA 82.1	1 viol.	✓ Clean	`C[C@@H]1[C@@H](C[C@@H]2[C@@H]1C[C@@]3([C@@H]4C[…`

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
ZINC104869865	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481	0.836	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC12501413	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2159505	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496	0.770	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2046807	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)[n…`
ZINC2125635	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O)[…`
ZINC21999938	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)[n…`
ZINC2583634	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)[n…`
ZINC4028557	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[nH…`
ZINC4557135	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)[n…`
ZINC4557136	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)[…`
ZINC4557137	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC5765081	0.681	258.2 Da LogP -2.54 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)[…`
ZINC71774763	0.671	432.3 Da LogP -2.23 TPSA 198.3	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@](=O)(O)N3CCOCC3…`
ZINC4602228	0.667	288.3 Da LogP -3.18 TPSA 145.0	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H](O)[C@H]2…`
ZINC4602229	0.667	288.3 Da LogP -3.18 TPSA 145.0	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H](O)[C@H]…`
ZINC4602233	0.667	288.3 Da LogP -3.18 TPSA 145.0	✓ Ro5	✓ Clean	`Cc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H](O)[C@@H]…`
ZINC4602235	0.667	288.3 Da LogP -3.18 TPSA 145.0	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H](O)[C@@H…`
ZINC4743771	0.652	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC4743772	0.652	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC4743774	0.652	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC4743775	0.652	361.3 Da LogP -2.70 TPSA 182.6	1 viol.	✓ Clean	`CS(=O)(=O)OC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC44430825	0.648	492.6 Da LogP 2.41 TPSA 122.5	✓ Ro5	✓ Clean	`CO[C@H]1[C@@H](O)[C@H](O)[C@H](OC[C@@]23C[C@@H]…`
ZINC12503703	0.638	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC8215878	0.638	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O…`
ZINC11422512	0.636	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](OP(=O)(O)O)[C@@H](COP(=O)(O)…`
ZINC100058967	0.632	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@H](CO[P@](=O)(O)OP(=O)…`
ZINC12504287	0.632	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC12504288	0.632	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC31308647	0.632	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc(=O)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(…`
ZINC1532637	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c…`
ZINC1550030	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c…`
ZINC1570863	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(…`
ZINC1698205	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c…`
ZINC4990801	0.629	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(=O)[nH]c(N)nc32)[C@@H](…`
ZINC5605239	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c…`
ZINC8613125	0.629	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c…`
ZINC97973759	0.629	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](O…`

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.