Protein profile

KP13_02275

Bifunctional protein aas

Genome: KpKP13

Gene: AHE42848.1 aas Structure source: AlphaFold + ColabFold UniProt A0A0H3GX39

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Amino acids 719

Annotations 8

Features 27

PDB binders 8

Druggability 0.949

Overview

Basic information about this protein and its source genome.

Accession: KP13_02275
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42848.1 aas
Status: annotated
Amino acids: 719
Structure source: AlphaFold + ColabFold

GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor). GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. GO:0008654 The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester. GO:0008779 Catalysis of the reaction: acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier protein] + O-(1-beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine. GO:0008922 Catalysis of the reaction: a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate. A long-chain fatty acid has an aliphatic tail containing 13 to 22 carbons. GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 36.986
Human E-value: 2.41e-08
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 91.22

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 0.949

Structure A0A0H3GX39

Pocket Pocket 38

P2Rank 0.915

Structure A0A0H3GX39

Pocket Pocket 1

ColabFold model

FPocket 0.944 · Pocket 48

P2Rank 0.959 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 109 / 4744 genomes with a hit

Normalized 0.023

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
GO:0008654 The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester.
GO:0008779 Catalysis of the reaction: acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier protein] + O-(1-beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine.
GO:0008922 Catalysis of the reaction: a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate. A long-chain fatty acid has an aliphatic tail containing 13 to 22 carbons.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0031956 Catalysis of the reaction: a medium-chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate. A medium-chain fatty acid has an aliphatic tail containing 6 to 12 carbons.

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
7	188	CDD	cd07989	LPLAT_AGPAT-like
370	381	ProSitePatterns	PS00455	Putative AMP-binding domain signature.
370	381	InterPro	IPR020845	AMP-binding, conserved site
39	58	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	15	Phobius	SIGNAL_PEPTIDE	Signal peptide region
16	38	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
211	612	Gene3D	G3DSA:3.40.50.12780	-
211	612	InterPro	IPR042099	ANL, N-terminal domain
278	719	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
59	257	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
30	140	SMART	SM00563	plsc_2
30	140	InterPro	IPR002123	Phospholipid/glycerol acyltransferase
1	717	Hamap	MF_01162	Bifunctional protein Aas [aas].
1	717	InterPro	IPR023775	Bifunctional protein Aas
10	170	SUPERFAMILY	SSF69593	Glycerol-3-phosphate (1)-acyltransferase
258	277	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
2	10	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
96	701	PANTHER	PTHR43201	ACYL-COA SYNTHETASE
1	1	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
231	619	Pfam	PF00501	AMP-binding enzyme
231	619	InterPro	IPR000873	AMP-dependent synthetase/ligase domain
16	137	Pfam	PF01553	Acyltransferase
16	137	InterPro	IPR002123	Phospholipid/glycerol acyltransferase
203	713	SUPERFAMILY	SSF56801	Acetyl-CoA synthetase-like
11	15	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
615	717	Gene3D	G3DSA:3.30.300.30	-
615	717	InterPro	IPR045851	AMP-binding enzyme, C-terminal domain superfamily

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_A0A0H3GX39	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02275	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
38				0.949

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	25.89	0.909
2	18.07	0.814
3	12.2	0.642
4	8.48	0.453
5	4.32	0.179

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
48				0.944
47				0.369
1				0.348

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	25.9	0.909
2	19.88	0.846
3	10.37	0.557
4	7.58	0.4
5	4.13	0.167

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.

64 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
3UK	5OE3	Q9I4X3	466.3 Da LogP -0.42 TPSA 218.2	1 viol.	✓ Clean	`c1ccc(c(c1)C(=O)OP(=O)(O)OC[C@@H]2[C@H]([C@H]([…`
9SN	5OE6	Q9I4X3	484.3 Da LogP -0.28 TPSA 218.2	1 viol.	✓ Clean	`c1cc(c(c(c1)F)C(=O)OP(=O)(O)OC[C@@H]2[C@H]([C@H…`
JSA	5ZRN	P9WQ37	530.6 Da LogP 1.12 TPSA 194.9	2 viol.	✓ Clean	`CCCCCCCCCCC[C@H](NS(=O)(=O)OC[C@@H]1[C@H]([C@H]…`
MCA	3NYQ	Q9L0A2	867.6 Da LogP -1.61 TPSA 400.9	3 viol.	✓ Clean	`C[C@H](C(=O)O)C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)…`
MLC	3NYR	Q9L0A2	853.6 Da LogP -1.86 TPSA 400.9	3 viol.	✓ Clean	`CC(C)(CO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]…`
MLI	3R44	P9WQ37	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
OXD	5IE3	Q9SMT7	90.0 Da LogP -0.84 TPSA 74.6	✓ Ro5	✓ Clean	`C(=O)(C(=O)O)O`
SRT	5IE0	Q9SMT7	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@H](C(=O)O)O)(C(=O)O)O`

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
CHEMBL371502	Q9I4X3	7.06	466.4 Da LogP -1.58 TPSA 212.0	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COS(=O)(=O)NC(=O)c2…`
CHEMBL377483	Q9I4X3	6.96	465.4 Da LogP -2.00 TPSA 214.8	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CNS(=O)(=O)NC(=O)c2…`
CHEMBL1315633	Q94696	—	365.2 Da LogP -2.69 TPSA 217.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
CHEMBL1326967	Q94696	—	226.3 Da LogP 3.55 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccccc3)sc2c1`
CHEMBL1375740	Q94696	—	255.3 Da LogP 2.95 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1F`
CHEMBL3392220	Q94696	—	448.4 Da LogP -0.51 TPSA 189.3	1 viol.	✓ Clean	`CCN(CC)CC.Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O…`

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
ZINC361067	1.000	226.3 Da LogP 3.55 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccccc3)sc2c1`
ZINC225954	0.806	241.3 Da LogP 3.13 TPSA 64.9	✓ Ro5	✓ Clean	`Nc1ccc(-c2nc3ccc(N)cc3s2)cc1`
ZINC235533	0.788	241.3 Da LogP 3.13 TPSA 64.9	✓ Ro5	✓ Clean	`Nc1cccc(-c2nc3ccc(N)cc3s2)c1`
ZINC8345430	0.750	312.3 Da LogP 2.07 TPSA 86.9	✓ Ro5	✓ Clean	`O=C(CNC(=O)c1ccccc1F)Nc1nc2ccccc2[nH]1`
ZINC381794	0.744	253.3 Da LogP 2.52 TPSA 78.0	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1O`
ZINC405324	0.744	271.7 Da LogP 3.47 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1Cl`
ZINC4538149	0.735	227.3 Da LogP 2.94 TPSA 51.8	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccncc3)sc2c1`
ZINC6653557	0.721	309.2 Da LogP 3.37 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(F)c(F)c(F)c1F`
ZINC235507	0.714	242.3 Da LogP 3.25 TPSA 59.1	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccc(O)cc3)sc2c1`
ZINC5589186	0.714	260.7 Da LogP 4.20 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3ccc(Cl)cc3)sc2c1`
ZINC13218513	0.707	316.2 Da LogP 3.58 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1Br`
ZINC441673	0.707	251.3 Da LogP 3.12 TPSA 57.8	✓ Ro5	✓ Clean	`Cc1ccccc1C(=O)Nc1nc2ccccc2[nH]1`
ZINC6506834	0.707	363.2 Da LogP 3.42 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1I`
ZINC12589519	0.705	307.7 Da LogP 3.75 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(F)c(F)cc1Cl`
ZINC4245368	0.703	227.3 Da LogP 2.94 TPSA 51.8	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3cccnc3)sc2c1`
ZINC4245370	0.703	242.3 Da LogP 3.25 TPSA 59.1	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3cccc(O)c3)sc2c1`
ZINC62538947	0.703	260.7 Da LogP 4.20 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc2nc(-c3cccc(Cl)c3)sc2c1`
ZINC12546511	0.698	305.3 Da LogP 3.83 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1C(F)(F)F`
ZINC12359024	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC12588992	0.690	306.2 Da LogP 4.12 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cccc(Cl)c1Cl`
ZINC13218630	0.690	287.3 Da LogP 3.97 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cccc2ccccc12`
ZINC17304201	0.689	324.1 Da LogP 4.26 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(F)c(Cl)cc1Cl`
ZINC9115469	0.681	285.3 Da LogP 2.96 TPSA 67.0	✓ Ro5	✓ Clean	`COc1ccc(C(=O)Nc2nc3ccccc3[nH]2)c(F)c1`
ZINC6589933	0.674	341.4 Da LogP 4.05 TPSA 74.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1C(=O)c1ccccc1`
ZINC12544692	0.667	330.4 Da LogP 2.19 TPSA 103.9	✓ Ro5	✓ Clean	`CS(=O)(=O)Nc1ccccc1C(=O)Nc1nc2ccccc2[nH]1`
ZINC12538671	0.659	306.2 Da LogP 4.12 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(Cl)ccc1Cl`
ZINC13228399	0.659	265.3 Da LogP 3.43 TPSA 57.8	✓ Ro5	✓ Clean	`Cc1cccc(C(=O)Nc2nc3ccccc3[nH]2)c1C`
ZINC14048562	0.659	270.3 Da LogP 2.50 TPSA 70.7	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cccnc1S`
ZINC406618	0.659	267.3 Da LogP 2.82 TPSA 67.0	✓ Ro5	✓ Clean	`COc1ccccc1C(=O)Nc1nc2ccccc2[nH]1`
ZINC9910431	0.659	273.2 Da LogP 3.09 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccc(F)c(F)c1`
ZINC1595024	0.657	245.7 Da LogP 4.62 TPSA 12.9	✓ Ro5	✓ Clean	`Clc1ccc2nc(-c3ccccc3)sc2c1`
ZINC1682939	0.657	229.3 Da LogP 4.10 TPSA 12.9	✓ Ro5	✓ Clean	`Fc1ccc2nc(-c3ccccc3)sc2c1`
ZINC29413288	0.657	227.3 Da LogP 3.67 TPSA 33.1	✓ Ro5	✓ Clean	`Oc1ccc2nc(-c3ccccc3)sc2c1`
ZINC402244	0.657	225.3 Da LogP 4.27 TPSA 12.9	✓ Ro5	✓ Clean	`Cc1ccc2nc(-c3ccccc3)sc2c1`
ZINC73638544	0.657	290.2 Da LogP 4.73 TPSA 12.9	✓ Ro5	✓ Clean	`Brc1ccc2nc(-c3ccccc3)sc2c1`
ZINC12603357	0.652	289.7 Da LogP 3.61 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccc(F)cc1Cl`
ZINC17304200	0.652	334.1 Da LogP 3.72 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccc(F)cc1Br`
ZINC6567101	0.652	303.3 Da LogP 3.42 TPSA 67.0	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1ccccc1OC(F)F`
ZINC72704	0.652	331.4 Da LogP 4.62 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1ccc(-c2nc3ccccc3[nH]2)cc1)c1ccccc1F`
ZINC6566971	0.651	273.2 Da LogP 3.09 TPSA 57.8	✓ Ro5	✓ Clean	`O=C(Nc1nc2ccccc2[nH]1)c1cc(F)cc(F)c1`
ZINC936069043	0.649	459.5 Da LogP -2.22 TPSA 217.8	1 viol.	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C…`
ZINC6299	0.647	226.3 Da LogP 3.55 TPSA 38.9	✓ Ro5	✓ Clean	`Nc1ccc(-c2nc3ccccc3s2)cc1`

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.