Protein profile

KP13_03760

Elongation factor G 1

Genome: KpKP13

Gene: AHE43703.1 fusA1 Structure source: AlphaFold + ColabFold UniProt A0A0H3H0I2
Amino acids 700
Annotations 7
Features 65
PDB binders 3
Druggability 0.557

Overview

Basic information about this protein and its source genome.

Accession
KP13_03760
Gene
AHE43703.1 fusA1
Status
annotated
Amino acids
700
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
60.0
Human E-value
1.92e-14
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
71.143
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
90.63

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 0.557
Structure A0A0H3H0I2
Pocket Pocket 4
P2Rank 0.646
Structure A0A0H3H0I2
Pocket Pocket 1
ColabFold model
FPocket 0.738 · Pocket 32
P2Rank 0.473 · Pocket 1
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 3663 / 4744 genomes with a hit
Normalized 0.772

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7
  • 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
609 686 CDD cd03713 EFG_mtEFG_C
609 686 InterPro IPR035649 EFG, domain V
329 396 Pfam PF03144 Elongation factor Tu domain 2
329 396 InterPro IPR004161 Translation elongation factor EFTu-like, domain 2
484 605 SUPERFAMILY SSF54211 Ribosomal protein S5 domain 2-like
484 605 InterPro IPR020568 Ribosomal protein S5 domain 2-type fold
8 290 ProSiteProfiles PS51722 Translational (tr)-type guanine nucleotide-binding (G) domain profile.
8 290 InterPro IPR000795 Translational (tr)-type GTP-binding domain
297 412 FunFam G3DSA:2.40.30.10:FF:000006 Elongation factor G
300 411 Gene3D G3DSA:2.40.30.10 Translation factors
137 146 PRINTS PR00315 GTP-binding elongation factor signature
137 146 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
85 95 PRINTS PR00315 GTP-binding elongation factor signature
85 95 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
101 112 PRINTS PR00315 GTP-binding elongation factor signature
101 112 InterPro IPR000795 Translational (tr)-type GTP-binding domain
485 604 SMART SM00889 EFG_IV_2
485 604 InterPro IPR005517 Translation elongation factor EFG/EF2, domain IV
609 696 SUPERFAMILY SSF54980 EF-G C-terminal domain-like
609 696 InterPro IPR035647 EF-G domain III/V-like
413 489 FunFam G3DSA:3.30.70.870:FF:000001 Elongation factor G
271 409 SUPERFAMILY SSF50447 Translation proteins
271 409 InterPro IPR009000 Translation protein, beta-barrel domain superfamily
51 66 ProSitePatterns PS00301 Translational (tr)-type guanine nucleotide-binding (G) domain signature.
51 66 InterPro IPR031157 Tr-type G domain, conserved site
610 680 Gene3D G3DSA:3.30.70.240 -
315 397 CDD cd04088 EFG_mtEFG_II
1 697 NCBIfam TIGR00484 elongation factor G
1 697 InterPro IPR004540 Translation elongation factor EFG/EF2
12 289 CDD cd01886 EF-G
488 603 CDD cd01434 EFG_mtEFG1_IV
488 603 InterPro IPR005517 Translation elongation factor EFG/EF2, domain IV
490 622 FunFam G3DSA:3.30.230.10:FF:000003 Elongation factor G
9 187 NCBIfam TIGR00231 small GTP-binding protein domain
9 187 InterPro IPR005225 Small GTP-binding protein domain
1 299 Gene3D G3DSA:3.40.50.300 -
1 299 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
407 485 SUPERFAMILY SSF54980 EF-G C-terminal domain-like
407 485 InterPro IPR035647 EF-G domain III/V-like
6 697 Hamap MF_00054_B Elongation factor G [fusA].
6 697 InterPro IPR004540 Translation elongation factor EFG/EF2
607 692 Pfam PF00679 Elongation factor G C-terminus
607 692 InterPro IPR000640 Elongation factor EFG, domain V-like
6 288 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
6 288 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
412 485 Gene3D G3DSA:3.30.70.870 Elongation Factor G (Translational Gtpase), domain 3
4 697 PANTHER PTHR43261 TRANSLATION ELONGATION FACTOR G-RELATED
606 693 SMART SM00838 EFG_C_a
606 693 InterPro IPR000640 Elongation factor EFG, domain V-like
1 299 FunFam G3DSA:3.40.50.300:FF:000029 Elongation factor G
489 694 Gene3D G3DSA:3.30.230.10 -
489 694 InterPro IPR014721 Ribosomal protein S5 domain 2-type fold, subgroup
410 485 CDD cd16262 EFG_III
410 485 InterPro IPR009022 Elongation factor G, domain III
610 680 FunFam G3DSA:3.30.70.240:FF:000001 Elongation factor G
9 288 Pfam PF00009 Elongation factor Tu GTP binding domain
9 288 InterPro IPR000795 Translational (tr)-type GTP-binding domain
409 482 Pfam PF14492 Elongation Factor G, domain III
409 482 InterPro IPR041095 Elongation Factor G, domain II
484 603 Pfam PF03764 Elongation factor G, domain IV
484 603 InterPro IPR005517 Translation elongation factor EFG/EF2, domain IV

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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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_A0A0H3H0I2
AlphaFold full sequence Viewing
ColabFold KP13_03760
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
1 0.017
6 0.004
5 0.002
52 0.002

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 Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 14.62 0.646
2 10.02 0.463
3 7.82 0.349
4 7.65 0.34
5 4.12 0.136

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.

54 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
FUA 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 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 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…

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.