Protein profile

PA4277

elongation factor Tu

Genome: NC_002516.2

Gene: tufB PA4265; PA4277 tufA Structure source: AlphaFold UniProt P09591

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Amino acids 397

Annotations 7

Features 43

PDB binders 11

Druggability 0.236

Overview

Basic information about this protein and its source genome.

Accession: PA4277
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: tufB PA4265; PA4277 tufA
Status: annotated
Amino acids: 397
Structure source: AlphaFold

3.6.5.3

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005525 Binding to GTP, guanosine triphosphate. GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. GO:0000287 Binding to a magnesium (Mg) ion. GO:0003746 Functions in chain elongation during polypeptide synthesis at the ribosome. GO:0006414 The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 81.818
Human E-value: 1.19e-10
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

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 0.236

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

3.6.5.3

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005525 Binding to GTP, guanosine triphosphate.
GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0003746 Functions in chain elongation during polypeptide synthesis at the ribosome.
GO:0006414 The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
301	395	Pfam	PF03143	Elongation factor Tu C-terminal domain
301	395	InterPro	IPR004160	Translation elongation factor EFTu/EF1A, C-terminal
303	392	CDD	cd03707	EFTU_III
208	304	SUPERFAMILY	SSF50447	Translation proteins
208	304	InterPro	IPR009000	Translation protein, beta-barrel domain superfamily
209	337	Gene3D	G3DSA:2.40.30.10	Translation factors
3	396	PANTHER	PTHR43721	ELONGATION FACTOR TU-RELATED
1	206	FunFam	G3DSA:3.40.50.300:FF:000003	Elongation factor Tu
10	207	ProSiteProfiles	PS51722	Translational (tr)-type guanine nucleotide-binding (G) domain profile.
10	207	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
13	147	NCBIfam	TIGR00231	small GTP-binding protein domain
13	147	InterPro	IPR005225	Small GTP-binding protein domain
10	204	Pfam	PF00009	Elongation factor Tu GTP binding domain
10	204	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
228	296	Pfam	PF03144	Elongation factor Tu domain 2
228	296	InterPro	IPR004161	Translation elongation factor EFTu-like, domain 2
341	396	Gene3D	G3DSA:2.40.30.10	Translation factors
94	105	PRINTS	PR00315	GTP-binding elongation factor signature
94	105	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
131	140	PRINTS	PR00315	GTP-binding elongation factor signature
131	140	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
78	88	PRINTS	PR00315	GTP-binding elongation factor signature
78	88	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
58	66	PRINTS	PR00315	GTP-binding elongation factor signature
58	66	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
14	27	PRINTS	PR00315	GTP-binding elongation factor signature
14	27	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
1	397	NCBIfam	TIGR00485	elongation factor Tu
1	397	InterPro	IPR004541	Translation elongation factor EFTu/EF1A, bacterial/organelle
1	397	Hamap	MF_00118_B	Elongation factor Tu [tuf].
6	222	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
6	222	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
11	206	CDD	cd01884	EF_Tu
11	206	InterPro	IPR041709	Elongation factor Tu (EF-Tu), GTP-binding domain
209	337	FunFam	G3DSA:2.40.30.10:FF:000001	Elongation factor Tu
301	396	SUPERFAMILY	SSF50465	EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
301	396	InterPro	IPR009001	Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal
51	66	ProSitePatterns	PS00301	Translational (tr)-type guanine nucleotide-binding (G) domain signature.
51	66	InterPro	IPR031157	Tr-type G domain, conserved site
214	300	CDD	cd03697	EFTU_II
214	300	InterPro	IPR033720	Elongation factor Tu, domain 2
1	206	Gene3D	G3DSA:3.40.50.300	-
1	206	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase

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 PA4277	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				0.236

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.

61 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
1MG	5AFI	P0CE48	377.3 Da LogP -2.56 TPSA 195.2	1 viol.	✓ Clean	`CN1C(=O)c2c(n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
5MU	5AFI	P0CE48	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)…`
GCP	5UYK	P0CE47	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…`
GLV	2HCJ	Q1R5Y2	74.0 Da LogP -0.73 TPSA 54.4	✓ Ro5	✓ Clean	`C(=O)C(=O)O`
GNP	4PC6	A0A0M3KKV1	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…`
KIR	5AFI	P0CE48	797.0 Da LogP 3.07 TPSA 228.1	3 viol.	✓ Clean	`CC[C@H](C(=O)NC\C=C\C=C(/C)\[C@H]([C@@H](C)[C@H…`
OGA	4IW3	Q88QP8	147.1 Da LogP -1.73 TPSA 103.7	✓ Ro5	✓ Clean	`C(C(=O)O)NC(=O)C(=O)O`
PSU	5AFI	P0CE48	324.2 Da LogP -2.67 TPSA 182.2	1 viol.	✓ Clean	`C1=C(C(=O)NC(=O)N1)[C@H]2[C@@H]([C@@H]([C@H](O2…`
PUL	4PC7	P0CE47	839.0 Da LogP 4.82 TPSA 198.5	2 viol.	✓ Clean	`C[C@@H]1[C@@H]([C@@H]([C@H]([C@@H](O1)O[C@@H](C…`
PXN	3MMP	P0CE48	368.5 Da LogP -0.44 TPSA 117.8	✓ Ro5	✓ Clean	`C[C@H](COCC(COC[C@@H](C)O)(COC[C@@H](C)O)COC[C@…`
TAC	2HCJ	Q1R5Y2	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`C[C@]1(c2cccc(c2C(=O)C3=C([C@]4([C@@H](C[C@@H]3…`

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
ZINC11525121	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC13515793	1.000	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]2…`
ZINC18202167	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC20410403	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC21984166	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC239173596	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4059755	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4215819	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3C…`
ZINC43771554	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4807269	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC575338663	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…`
ZINC84441937	1.000	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC13518650	0.837	418.2 Da LogP -2.31 TPSA 217.8	1 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[C…`
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)(…`
ZINC65748564	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC65748567	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC77312680	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC13519607	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)OP…`
ZINC31298140	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168754	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168756	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC28630683	0.800	444.4 Da LogP 0.84 TPSA 182.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(=N)O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC35051264	0.800	444.4 Da LogP 0.84 TPSA 182.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(=N)O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC71769623	0.793	417.4 Da LogP -0.78 TPSA 198.6	1 viol.	✓ Clean	`C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…`
ZINC71769624	0.793	417.4 Da LogP -0.78 TPSA 198.6	1 viol.	✓ Clean	`C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…`
ZINC71769638	0.793	416.4 Da LogP -0.82 TPSA 204.4	1 viol.	✓ Clean	`C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…`
ZINC113264413	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC113264415	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC2244337	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2244338	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)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)[…`
ZINC1834294	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@H](N)C(=O)O)c1)C(=O)O`
ZINC1834295	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC1834297	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC19701767	0.762	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC19701769	0.762	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`

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.