Protein profile

KP13_01023

Bifunctional protein folC

Genome: KpKP13

Gene: AHE43449.1 folC Structure source: AlphaFold + ColabFold UniProt A0A0H3GVS7
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Amino acids 422
Annotations 10
Features 24
PDB binders 7
Druggability 0.93

Overview

Basic information about this protein and its source genome.

Accession
KP13_01023
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE43449.1 folC
Status
annotated
Amino acids
422
Structure source
AlphaFold + ColabFold
GO
GO:0004326 Catalysis of the reaction: ATP + tetrahydrofolyl-(Glu)(n) + L-glutamate = ADP + phosphate + tetrahydrofolyl-(Glu)(n+1). 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:0016881 Catalysis of the ligation of an acid to an amino acid via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate. GO:0009396 The chemical reactions and pathways resulting in the formation of folic acid and its derivatives. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
37.43
Human E-value
2.53e-29
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
80.569
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
95.66

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 0.93
Structure A0A0H3GVS7
Pocket Pocket 3
P2Rank 0.967
Structure A0A0H3GVS7
Pocket Pocket 1
ColabFold model
FPocket 0.851 · Pocket 1
P2Rank 0.959 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 139 / 4744 genomes with a hit
Normalized 0.029

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

10 GO

Gene Ontology (GO)

10
  • GO:0004326 Catalysis of the reaction: ATP + tetrahydrofolyl-(Glu)(n) + L-glutamate = ADP + phosphate + tetrahydrofolyl-(Glu)(n+1).
  • 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:0016881 Catalysis of the ligation of an acid to an amino acid via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.
  • GO:0009396 The chemical reactions and pathways resulting in the formation of folic acid and its derivatives.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0008841 Catalysis of the reaction: ATP + dihydropterate + L-glutamate = ADP + phosphate + dihydrofolate.
  • GO:0046872 Binding to a metal ion.
  • GO:0046656 The chemical reactions and pathways resulting in the formation of folic acid, pteroylglutamic acid.
  • GO:0046654 The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records
Show feature table
Start End DB Term Name
287 353 Pfam PF02875 Mur ligase family, glutamate ligase domain
287 353 InterPro IPR004101 Mur ligase, C-terminal
7 418 PIRSF PIRSF001563 Folylpolyglu_synth
7 418 InterPro IPR001645 Folylpolyglutamate synthetase
3 287 Gene3D G3DSA:3.40.1190.10 -
3 287 InterPro IPR036565 Mur-like, catalytic domain superfamily
13 284 SUPERFAMILY SSF53623 MurD-like peptide ligases, catalytic domain
13 284 InterPro IPR036565 Mur-like, catalytic domain superfamily
144 159 ProSitePatterns PS01012 Folylpolyglutamate synthase signature 2.
144 159 InterPro IPR018109 Folylpolyglutamate synthetase, conserved site
54 196 Pfam PF08245 Mur ligase middle domain
54 196 InterPro IPR013221 Mur ligase, central
29 355 PANTHER PTHR11136 FOLYLPOLYGLUTAMATE SYNTHASE-RELATED
29 355 InterPro IPR001645 Folylpolyglutamate synthetase
8 287 FunFam G3DSA:3.40.1190.10:FF:000004 Dihydrofolate synthase/folylpolyglutamate synthase
288 420 Gene3D G3DSA:3.90.190.20 -
288 420 InterPro IPR036615 Mur ligase, C-terminal domain superfamily
288 416 FunFam G3DSA:3.90.190.20:FF:000005 Dihydrofolate synthase/folylpolyglutamate synthase
286 413 SUPERFAMILY SSF53244 MurD-like peptide ligases, peptide-binding domain
286 413 InterPro IPR036615 Mur ligase, C-terminal domain superfamily
32 413 NCBIfam TIGR01499 bifunctional protein FolC
32 413 InterPro IPR001645 Folylpolyglutamate synthetase
52 75 ProSitePatterns PS01011 Folylpolyglutamate synthase signature 1.
52 75 InterPro IPR018109 Folylpolyglutamate synthetase, conserved site

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_A0A0H3GVS7
AlphaFold — — full sequence — Viewing
ColabFold KP13_01023
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
3 0.93
10 0.638
6 0.243

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 25.64 0.908
2 6.17 0.307
3 0.62 0.0

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

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
ACP
1JBV
P15925 505.2 Da LogP -1.52 TPSA 269.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
ACQ
1JBW
P15925 585.2 Da LogP -1.40 TPSA 316.4 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
ANP
3QCZ
A0A5P8YIK0 506.2 Da LogP -2.06 TPSA 281.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
PD8
1W78
P08192 392.3 Da LogP 0.16 TPSA 193.4 ✓ Ro5 ✓ Clean c1cc(ccc1C(=O)OP(=O)(O)O)NCc2cnc3c(n2)C(=O)NC(=…
POP
1FGS
P15925 176.0 Da LogP -2.08 TPSA 129.9 ✓ Ro5 ✓ Clean O[P@@](=O)([O-])O[P@@](=O)(O)[O-]
TLA
3NRS
Q8D0U0 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=O)O)O
TMF
1JBW
P15925 455.4 Da LogP -0.23 TPSA 194.3 ✓ Ro5 ✓ Clean c1cc(ccc1C(=O)N[C@H](CCC(=O)O)C(=O)O)[N@@]2C[C@…

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.