Protein profile

KP13_00742

Elongation factor G

Genome: KpKP13

Gene: fusA AHE42359.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GWM9

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Amino acids 704

Annotations 7

Features 65

PDB binders 5

Druggability 0.675

Overview

Basic information about this protein and its source genome.

Accession: KP13_00742
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: fusA AHE42359.1
Status: annotated
Amino acids: 704
Structure source: AlphaFold + ColabFold

GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. GO:0003746 Functions in chain elongation during polypeptide synthesis at the ribosome. GO:0005525 Binding to GTP, guanosine triphosphate. GO:0006414 The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0097216 Binding to guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 57.895
Human E-value: 5.41e-13
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 98.58
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 90.73

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 0.675

Structure A0A0H3GWM9

Pocket Pocket 4

P2Rank 0.6

Structure A0A0H3GWM9

Pocket Pocket 1

ColabFold model

FPocket 0.701 · Pocket 9

P2Rank 0.548 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3670 / 4744 genomes with a hit

Normalized 0.774

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

GO:0003924 Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
GO:0003746 Functions in chain elongation during polypeptide synthesis at the ribosome.
GO:0005525 Binding to GTP, guanosine triphosphate.
GO:0006414 The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0097216 Binding to guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions.
GO:0032790 The disaggregation of a ribosome into its constituent components; includes the dissociation of ribosomal subunits.

Sequence Features

Domain/signature hits from InterPro and related databases.

65 records

Show feature table

Start	End	DB	Term	Name
1	298	Gene3D	G3DSA:3.40.50.300	-
1	298	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
3	702	PANTHER	PTHR43261	TRANSLATION ELONGATION FACTOR G-RELATED
415	491	Gene3D	G3DSA:3.30.70.870	Elongation Factor G (Translational Gtpase), domain 3
300	414	FunFam	G3DSA:2.40.30.10:FF:000006	Elongation factor G
317	399	CDD	cd04088	EFG_mtEFG_II
614	691	CDD	cd03713	EFG_mtEFG_C
614	691	InterPro	IPR035649	EFG, domain V
9	288	Pfam	PF00009	Elongation factor Tu GTP binding domain
9	288	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
1	703	NCBIfam	TIGR00484	elongation factor G
1	703	InterPro	IPR004540	Translation elongation factor EFG/EF2
1	299	FunFam	G3DSA:3.40.50.300:FF:000029	Elongation factor G
615	685	FunFam	G3DSA:3.30.70.240:FF:000001	Elongation factor G
411	485	Pfam	PF14492	Elongation Factor G, domain III
411	485	InterPro	IPR041095	Elongation Factor G, domain II
411	488	SUPERFAMILY	SSF54980	EF-G C-terminal domain-like
411	488	InterPro	IPR035647	EF-G domain III/V-like
299	414	Gene3D	G3DSA:2.40.30.10	Translation factors
51	66	ProSitePatterns	PS00301	Translational (tr)-type guanine nucleotide-binding (G) domain signature.
51	66	InterPro	IPR031157	Tr-type G domain, conserved site
6	702	Hamap	MF_00054_B	Elongation factor G [fusA].
6	702	InterPro	IPR004540	Translation elongation factor EFG/EF2
331	398	Pfam	PF03144	Elongation factor Tu domain 2
331	398	InterPro	IPR004161	Translation elongation factor EFTu-like, domain 2
611	700	SUPERFAMILY	SSF54980	EF-G C-terminal domain-like
611	700	InterPro	IPR035647	EF-G domain III/V-like
486	609	Pfam	PF03764	Elongation factor G, domain IV
486	609	InterPro	IPR005517	Translation elongation factor EFG/EF2, domain IV
12	289	CDD	cd01886	EF-G
490	609	CDD	cd01434	EFG_mtEFG1_IV
490	609	InterPro	IPR005517	Translation elongation factor EFG/EF2, domain IV
611	696	Pfam	PF00679	Elongation factor G C-terminus
611	696	InterPro	IPR000640	Elongation factor EFG, domain V-like
492	699	Gene3D	G3DSA:3.30.230.10	-
492	699	InterPro	IPR014721	Ribosomal protein S5 domain 2-type fold, subgroup
85	95	PRINTS	PR00315	GTP-binding elongation factor signature
85	95	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
137	146	PRINTS	PR00315	GTP-binding elongation factor signature
137	146	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
101	112	PRINTS	PR00315	GTP-binding elongation factor signature
101	112	InterPro	IPR000795	Translational (tr)-type GTP-binding domain
12	25	PRINTS	PR00315	GTP-binding elongation factor signature
12	25	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
487	609	SMART	SM00889	EFG_IV_2
487	609	InterPro	IPR005517	Translation elongation factor EFG/EF2, domain IV
412	487	CDD	cd16262	EFG_III
412	487	InterPro	IPR009022	Elongation factor G, domain III
615	685	Gene3D	G3DSA:3.30.70.240	-
486	610	SUPERFAMILY	SSF54211	Ribosomal protein S5 domain 2-like
486	610	InterPro	IPR020568	Ribosomal protein S5 domain 2-type fold
6	288	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
6	288	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
10	187	NCBIfam	TIGR00231	small GTP-binding protein domain
10	187	InterPro	IPR005225	Small GTP-binding protein domain
611	698	SMART	SM00838	EFG_C_a
611	698	InterPro	IPR000640	Elongation factor EFG, domain V-like
415	491	FunFam	G3DSA:3.30.70.870:FF:000001	Elongation factor G
271	411	SUPERFAMILY	SSF50447	Translation proteins
271	411	InterPro	IPR009000	Translation protein, beta-barrel domain superfamily
492	627	FunFam	G3DSA:3.30.230.10:FF:000003	Elongation factor G
8	290	ProSiteProfiles	PS51722	Translational (tr)-type guanine nucleotide-binding (G) domain profile.
8	290	InterPro	IPR000795	Translational (tr)-type GTP-binding domain

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...

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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_A0A0H3GWM9	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00742	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
4				0.675

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	10.78	0.578
2	5.81	0.283
3	5.54	0.265
4	5.38	0.255
5	4.51	0.192

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
9				0.701
25				0.286

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	9.41	0.506
2	6.79	0.347
3	5.02	0.228
4	4.58	0.197
5	3.13	0.106

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
5GP	6YDP	Q96RP9	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…`
FUA	4V7B	P0A6M8	516.7 Da LogP 5.67 TPSA 104.1	2 viol.	✓ Clean	`C[C@H]1[C@@H]2CC[C@]3([C@H]([C@]2(CC[C@H]1O)C)[…`
GCP	4V9O	P0A6M8	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	4V9J	Q5SHN5	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…`
SPM	6YDP	Q96RP9	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`C(CCNCCCN)CNCCCN`

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
CHEMBL1256987	P68790	—	538.7 Da LogP 1.34 TPSA 106.9	1 viol.	✓ Clean	`CC(=O)O[C@H]1C[C@@]2(C)[C@@H](C[C@@H](O)[C@H]3[…`

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
ZINC1532734	1.000	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCNCCCCNCCCN`
ZINC27564039	0.867	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCNCCCN`
ZINC13377742	0.857	230.4 Da LogP 0.42 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCCNCCCCN`
ZINC104869865	0.850	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	0.850	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	0.850	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	0.850	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	0.850	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	0.850	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	0.850	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)(…`
ZINC1598087	0.800	215.4 Da LogP 1.61 TPSA 64.1	✓ Ro5	✓ Clean	`NCCCCCCNCCCCCCN`
ZINC12501413	0.783	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	0.783	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	0.783	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	0.783	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	0.783	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	0.783	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	0.783	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	0.783	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	0.783	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)[…`
ZINC100056474	0.684	270.5 Da LogP 4.63 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCNCCCN`
ZINC59496006	0.684	242.5 Da LogP 3.85 TPSA 38.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNCCCN`
ZINC71774763	0.681	432.3 Da LogP -2.23 TPSA 198.3	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@](=O)(O)N3CCOCC3…`
ZINC4743771	0.662	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	0.662	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	0.662	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	0.662	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…`
ZINC12503703	0.647	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	0.647	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…`
ZINC100058967	0.642	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	0.642	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	0.642	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	0.642	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(…`
ZINC1674993	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSCCSCC[C@H](N)C(=O)O)C(=O)O`
ZINC1674994	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCSCCSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1674996	0.640	296.4 Da LogP 0.06 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCSCCSCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1532637	0.639	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	0.639	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	0.639	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…`
ZINC2020098	0.639	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(…`
ZINC38580950	0.639	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…`
ZINC3869968	0.639	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)…`
ZINC3869969	0.639	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)…`
ZINC4990799	0.639	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…`
ZINC4990800	0.639	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](…`
ZINC4990801	0.639	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](…`
ZINC4990802	0.639	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]…`
ZINC8613125	0.639	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	0.639	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…`
ZINC97973760	0.639	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](…`

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.