Protein profile

KP13_00780

Methionyl-tRNA formyltransferase

Genome: KpKP13

Gene: fmt AHE42393.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GU02
Amino acids 315
Annotations 6
Features 25
PDB binders 11
Druggability 0.607

Overview

Basic information about this protein and its source genome.

Accession
KP13_00780
Gene
fmt AHE42393.1
Status
annotated
Amino acids
315
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
35.625
Human E-value
1.17e-18
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
88.535
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
96.38

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 0.607
Structure A0A0H3GU02
Pocket Pocket 6
P2Rank 0.81
Structure A0A0H3GU02
Pocket Pocket 1
ColabFold model
FPocket 0.428 · Pocket 20
P2Rank 0.758 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 191 / 4744 genomes with a hit
Normalized 0.04

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

5
  • GO:0071951 The modification process that results in the conversion of methionine charged on a tRNA(fMet) to N-formyl-methionine-tRNA(fMet).
  • GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0004479 Catalysis of the reaction: 10-formyltetrahydrofolate + L-methionyl-tRNA + H2O = tetrahydrofolate + N-formylmethionyl-tRNA.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records
Show feature table
Start End DB Term Name
2 307 PANTHER PTHR11138 METHIONYL-TRNA FORMYLTRANSFERASE
210 315 FunFam G3DSA:3.10.25.10:FF:000001 Methionyl-tRNA formyltransferase
210 315 Gene3D G3DSA:3.10.25.10 -
210 315 InterPro IPR037022 Formyl transferase, C-terminal domain superfamily
5 307 Hamap MF_00182 Methionyl-tRNA formyltransferase [fmt].
5 307 InterPro IPR005794 Methionyl-tRNA formyltransferase
136 159 ProSitePatterns PS00373 Phosphoribosylglycinamide formyltransferase active site.
136 159 InterPro IPR001555 Phosphoribosylglycinamide formyltransferase, active site
6 183 Pfam PF00551 Formyl transferase
6 183 InterPro IPR002376 Formyl transferase, N-terminal
1 209 FunFam G3DSA:3.40.50.170:FF:000003 Methionyl-tRNA formyltransferase
5 308 NCBIfam TIGR00460 methionyl-tRNA formyltransferase
5 308 InterPro IPR005794 Methionyl-tRNA formyltransferase
4 206 SUPERFAMILY SSF53328 Formyltransferase
4 206 InterPro IPR036477 Formyl transferase, N-terminal domain superfamily
211 297 CDD cd08704 Met_tRNA_FMT_C
211 297 InterPro IPR044135 Methionyl-tRNA formyltransferase, C-terminal domain
208 309 SUPERFAMILY SSF50486 FMT C-terminal domain-like
208 309 InterPro IPR011034 Formyl transferase-like, C-terminal domain superfamily
207 304 Pfam PF02911 Formyl transferase, C-terminal domain
207 304 InterPro IPR005793 Formyl transferase, C-terminal
1 209 Gene3D G3DSA:3.40.50.170 -
5 208 CDD cd08646 FMT_core_Met-tRNA-FMT_N
5 208 InterPro IPR041711 Methionyl-tRNA formyltransferase, N-terminal domain
5 308 FunFam G3DSA:3.40.50.12230:FF:000001 Methionyl-tRNA formyltransferase

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_A0A0H3GU02
AlphaFold full sequence Viewing
ColabFold KP13_00780
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
6 0.607
17 0.011
1 0.007
3 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 21.43 0.81
2 0.92 0.004

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

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
1YA F8WJP6 473.4 Da LogP -0.73 TPSA 219.8 1 viol. ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)N(C[C@@H]…
1YJ F8WJP6 445.4 Da LogP -0.28 TPSA 211.6 1 viol. ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@@H]2…
6DD E3NZ06 467.4 Da LogP 1.13 TPSA 196.0 ✓ Ro5 ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)N(Cc2ccc3…
B62 F8WJP6 181.2 Da LogP -0.42 TPSA 95.8 ✓ Ro5 ✓ Clean C[C@@H]1CNC2=C(N1)C(=O)NC(=N2)N
BTB E3NZ06 209.2 Da LogP -3.01 TPSA 104.4 ✓ Ro5 ✓ Clean C(CO)N(CCO)C(CO)(CO)CO
FME P23882 177.2 Da LogP -0.06 TPSA 66.4 ✓ Ro5 ✓ Clean CSCC[C@@H](C(=O)O)NC=O
FON F8WJP6 473.4 Da LogP -0.73 TPSA 219.8 1 viol. ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@@H]2…
JB2 F8WJP6 588.4 Da LogP -3.63 TPSA 317.3 3 viol. ✓ Clean C[C@@H]1[C@H]([C@@H]([C@@H]([C@H](O1)OP(=O)(O)O…
MOE Q8ZJ80 75.1 Da LogP -1.01 TPSA 32.3 ✓ Ro5 ✓ Clean COCC[O-]
PG5 Q81WH2 178.2 Da LogP 0.31 TPSA 36.9 ✓ Ro5 ✓ Clean COCCOCCOCCOC
THG E3NZ06 445.4 Da LogP -0.28 TPSA 211.6 1 viol. ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@H]2C…

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.