Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: KP13_04206
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE45437.1 pflA
Status: annotated
Amino acids: 246
Structure source: AlphaFold + ColabFold

EC

1.97.1.4

GO

GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0043365 Catalysis of the reaction: S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. 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:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. 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: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 73.577
DEG E-value: 1.13e-131
Localization: Cytoplasmic
ColabFold pLDDT: 97.32

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 0.377

Structure A0A0H3GM98

Pocket Pocket 1

P2Rank 0.914

Structure A0A0H3GM98

Pocket Pocket 1

ColabFold model

FPocket 0.553 · Pocket 1

P2Rank 0.97 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 199 / 4744 genomes with a hit

Normalized 0.042

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

1.97.1.4

Gene Ontology (GO)

9

GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0043365 Catalysis of the reaction: S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
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:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
GO:0046872 Binding to a metal ion.
GO:0006006 The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
44	246	PIRSF	PIRSF000371	PFLA_YjjW
44	246	InterPro	IPR012839	Organic radical enzyme activase
1	47	PIRSF	PIRSF000371	PFLA_YjjW
1	47	InterPro	IPR012839	Organic radical enzyme activase
23	216	SUPERFAMILY	SSF102114	Radical SAM enzymes
18	39	ProSitePatterns	PS01087	Radical activating enzymes signature.
18	39	InterPro	IPR001989	Radical-activating enzyme, conserved site
16	239	ProSiteProfiles	PS51918	Radical SAM core domain profile.
16	239	InterPro	IPR007197	Radical SAM
5	246	PANTHER	PTHR30352	PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME
5	246	InterPro	IPR034457	Organic radical-activating enzymes
2	246	FunFam	G3DSA:3.20.20.70:FF:000050	Pyruvate formate-lyase-activating enzyme
3	243	SFLD	SFLDG01066	organic radical-activating enzymes
3	243	SFLD	SFLDF00278	pyruvate formate-lyase activase
3	243	InterPro	IPR034465	Pyruvate formate-lyase activase
6	239	NCBIfam	TIGR02493	pyruvate formate-lyase-activating protein
6	239	InterPro	IPR012838	Pyruvate formate-lyase 1 activating enzyme
24	208	CDD	cd01335	Radical_SAM
24	178	Pfam	PF04055	Radical SAM superfamily
24	178	InterPro	IPR007197	Radical SAM
2	246	Gene3D	G3DSA:3.20.20.70	Aldolase class I
2	246	InterPro	IPR013785	Aldolase-type TIM barrel
16	146	Pfam	PF13353	4Fe-4S single cluster 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_A0A0H3GM98	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_04206	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				0.377

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				19.42	0.839

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				0.553

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				31.38	0.939
2				1.9	0.038

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.

1 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
MT2	3C8F	P0A9N4	178.3 Da LogP 0.06 TPSA 63.3	✓ Ro5	✓ Clean	`CC[S@@+](C)CC[C@@H](C(=O)O)N`

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).

No virtual-screening candidates for this protein.

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.

KP13_04206

Overview

Target profile

Selected Druggability evidence

Sequence

Functional Annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence Features

3D Structure

Structural evidence

Pockets (FPOCKET)

Pockets (P2RANK)

Pockets (FPOCKET)

Pockets (P2RANK)

Ligand evidence