Protein profile

KP13_01718

Phospholipase A1 bifunctional protein

Genome: KpKP13

Gene: AHE46978.1 pldA Structure source: AlphaFold + ColabFold UniProt A0A0H3GGK3

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Amino acids 286

Annotations 10

Features 34

PDB binders 1

Druggability 0.67

Overview

Basic information about this protein and its source genome.

Accession: KP13_01718
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE46978.1 pldA
Status: annotated
Amino acids: 286
Structure source: AlphaFold + ColabFold

3.1.1.32 3.1.1.4

GO:0004620 Catalysis of the hydrolysis of a glycerophospholipid. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0006629 The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids. GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures. GO:0005509 Binding to a calcium ion (Ca2+). GO:0008970 Catalysis of the reaction: a 1,2-diacyl-sn-glycero-3-phospholipid + H2O = a 2-acyl-sn-glycero-3-phospholipid + a fatty acid + H+. Note that the substrate has a diacyl group attached to the glycerol group.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: OuterMembrane
ColabFold pLDDT: 92.34

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 0.67

Structure A0A0H3GGK3

Pocket Pocket 8

P2Rank 0.909

Structure A0A0H3GGK3

Pocket Pocket 1

ColabFold model

FPocket 0.974 · Pocket 25

P2Rank 0.903 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 104 / 4744 genomes with a hit

Normalized 0.022

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 8 GO

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0004620 Catalysis of the hydrolysis of a glycerophospholipid.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0006629 The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.
GO:0005509 Binding to a calcium ion (Ca2+).
GO:0008970 Catalysis of the reaction: a 1,2-diacyl-sn-glycero-3-phospholipid + H2O = a 2-acyl-sn-glycero-3-phospholipid + a fatty acid + H+. Note that the substrate has a diacyl group attached to the glycerol group.
GO:0004623 A glycerophospholipase activity that cleaves the fatty acid attached to the sn-2 position of the glycerol group of a glycerophospholipid. Substrates include phosphatidylcholine, phosphatidylethanolamine, choline plasmalogen and phosphatides.
GO:0016042 The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.

Sequence Features

Domain/signature hits from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
37	285	SUPERFAMILY	SSF56931	Outer membrane phospholipase A (OMPLA)
37	285	InterPro	IPR036541	Phospholipase A1 superfamily
47	277	CDD	cd00541	OMPLA
47	277	InterPro	IPR003187	Phospholipase A1
41	282	Pfam	PF02253	Phospholipase A1
41	282	InterPro	IPR003187	Phospholipase A1
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
30	286	Gene3D	G3DSA:2.40.230.10	Phospholipase A1
30	286	InterPro	IPR036541	Phospholipase A1 superfamily
1	2	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
24	286	PANTHER	PTHR40457	PHOSPHOLIPASE A1
24	286	InterPro	IPR003187	Phospholipase A1
153	167	PRINTS	PR01486	Bacterial phospholipase A1 protein signature
153	167	InterPro	IPR003187	Phospholipase A1
123	142	PRINTS	PR01486	Bacterial phospholipase A1 protein signature
123	142	InterPro	IPR003187	Phospholipase A1
233	250	PRINTS	PR01486	Bacterial phospholipase A1 protein signature
233	250	InterPro	IPR003187	Phospholipase A1
100	116	PRINTS	PR01486	Bacterial phospholipase A1 protein signature
100	116	InterPro	IPR003187	Phospholipase A1
200	218	PRINTS	PR01486	Bacterial phospholipase A1 protein signature
200	218	InterPro	IPR003187	Phospholipase A1
168	186	PRINTS	PR01486	Bacterial phospholipase A1 protein signature
168	186	InterPro	IPR003187	Phospholipase A1
255	275	PRINTS	PR01486	Bacterial phospholipase A1 protein signature
255	275	InterPro	IPR003187	Phospholipase A1
78	95	PRINTS	PR01486	Bacterial phospholipase A1 protein signature
78	95	InterPro	IPR003187	Phospholipase A1
30	286	FunFam	G3DSA:2.40.230.10:FF:000001	Phospholipase A(1)
1	20	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
21	286	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
15	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	22	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
3	14	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.

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_A0A0H3GGK3	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01718	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
8				0.67
5				0.395
14				0.309

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	19.93	0.847
2	2.9	0.092
3	1.38	0.017

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
25				0.974

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	19.22	0.836
2	2.71	0.081
3	2.0	0.043
4	0.81	0.003

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.

51 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
HDS	1QD6	P0A921	306.5 Da LogP 5.36 TPSA 54.4	1 viol.	✓ Clean	`CCCCCCCCCCCCCCCCS(=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).

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).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC100019805	1.000	292.5 Da LogP 4.97 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCS(=O)(=O)O`
ZINC1625794	1.000	264.4 Da LogP 4.19 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCS(=O)(=O)O`
ZINC1651926	1.000	250.4 Da LogP 3.80 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCS(=O)(=O)O`
ZINC1843748	1.000	222.3 Da LogP 3.01 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCS(=O)(=O)O`
ZINC2515939	1.000	236.4 Da LogP 3.41 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCS(=O)(=O)O`
ZINC42921009	1.000	278.5 Da LogP 4.58 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCS(=O)(=O)O`
ZINC80135680	1.000	208.3 Da LogP 2.62 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCS(=O)(=O)O`
ZINC5113156	0.722	246.3 Da LogP 0.32 TPSA 108.7	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCCCS(=O)(=O)O`
ZINC1763010	0.667	218.3 Da LogP -0.46 TPSA 108.7	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCS(=O)(=O)O`
ZINC14880434	0.654	336.6 Da LogP 4.26 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC2384686	0.654	280.5 Da LogP 2.70 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC58541260	0.654	308.5 Da LogP 3.48 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC[N+](C)(C)CCCS(=O)(=O)O`
ZINC20231719	0.619	234.4 Da LogP 3.56 TPSA 34.1	✓ Ro5	✓ Clean	`CCCCCCS(=O)(=O)CCCCCC`
ZINC2166283	0.619	262.5 Da LogP 4.34 TPSA 34.1	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)CCCCCC`
ZINC104242223	0.615	322.5 Da LogP 4.59 TPSA 63.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCS(=O)(=O)O`
ZINC1589373	0.615	238.3 Da LogP 2.25 TPSA 63.6	✓ Ro5	✓ Clean	`CCCCCCCCOCCS(=O)(=O)O`
ZINC1595574	0.591	234.4 Da LogP 3.56 TPSA 34.1	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)CCCC`
ZINC1595597	0.591	220.4 Da LogP 3.17 TPSA 34.1	✓ Ro5	✓ Clean	`CCCCCCCCCCS(C)(=O)=O`
ZINC5225211	0.579	204.2 Da LogP -0.85 TPSA 108.7	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCS(=O)(=O)O`
ZINC1690090	0.571	206.4 Da LogP 2.78 TPSA 34.1	✓ Ro5	✓ Clean	`CCCCCS(=O)(=O)CCCCC`
ZINC59471161	0.565	265.4 Da LogP 2.73 TPSA 80.4	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCS(=O)(=O)O`
ZINC100310228	0.560	334.6 Da LogP 4.87 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCS(=O)(=O)CCO`
ZINC101020164	0.560	292.5 Da LogP 3.70 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCS(=O)(=O)CCCO`
ZINC1732769	0.560	222.3 Da LogP 1.75 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)CCO`
ZINC98008412	0.560	250.4 Da LogP 2.53 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)CCCCO`
ZINC98008415	0.560	236.4 Da LogP 2.14 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)CCCO`
ZINC2895764	0.533	279.4 Da LogP 2.13 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)NCCS(=O)(=O)O`
ZINC59696283	0.533	363.6 Da LogP 4.47 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)NCCS(=O)(=O)O`
ZINC95669587	0.533	308.4 Da LogP 3.34 TPSA 80.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCS(=O)(=O)O`
ZINC1593660	0.520	221.4 Da LogP 2.24 TPSA 37.4	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)N(C)C`
ZINC1602586	0.520	207.3 Da LogP 1.90 TPSA 46.2	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)NC`
ZINC97977037	0.520	278.5 Da LogP 4.27 TPSA 43.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCS(=O)(=O)OC`
ZINC100311643	0.519	292.4 Da LogP 3.41 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCS(=O)(=O)CC(=O)O`
ZINC1583652	0.519	264.4 Da LogP 2.63 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCCCCCS(=O)(=O)CC(=O)O`
ZINC20519776	0.519	208.3 Da LogP 1.07 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCS(=O)(=O)CC(=O)O`
ZINC43352221	0.519	236.3 Da LogP 1.85 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)CC(=O)O`
ZINC116083549	0.517	224.3 Da LogP 1.00 TPSA 80.7	✓ Ro5	✓ Clean	`CCOC(=O)CCCCCS(=O)(=O)O`
ZINC100025293	0.516	262.4 Da LogP 1.50 TPSA 60.9	✓ Ro5	✓ Clean	`CCCCN1C=CN(CCCCS(=O)(=O)O)C1`
ZINC100304321	0.516	349.5 Da LogP 4.03 TPSA 74.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)N(C)CCS(=O)(=O)O`
ZINC59684305	0.516	321.5 Da LogP 3.25 TPSA 74.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)N(C)CCS(=O)(=O)O`
ZINC103008613	0.500	249.4 Da LogP 3.07 TPSA 46.2	✓ Ro5	✓ Clean	`CCCCCCCCCNS(=O)(=O)CCC`
ZINC1550780	0.500	235.3 Da LogP 1.25 TPSA 77.2	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)CC(N)=O`
ZINC1602573	0.500	222.3 Da LogP 2.71 TPSA 43.4	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)OCC`
ZINC1723787	0.500	204.3 Da LogP 2.91 TPSA 34.1	✓ Ro5	✓ Clean	`C=CS(=O)(=O)CCCCCCCC`
ZINC1847701	0.500	238.3 Da LogP 2.95 TPSA 63.6	✓ Ro5	✓ Clean	`CCCCCCCCCCOS(=O)(=O)O`
ZINC2004468	0.500	224.3 Da LogP 2.56 TPSA 63.6	✓ Ro5	✓ Clean	`CCCCCCCCCOS(=O)(=O)O`
ZINC2015925	0.500	210.3 Da LogP 2.17 TPSA 63.6	✓ Ro5	✓ Clean	`CCCCCCCCOS(=O)(=O)O`
ZINC2865194	0.500	221.4 Da LogP 1.72 TPSA 60.2	✓ Ro5	✓ Clean	`CCCCCCCCS(=O)(=O)CCN`
ZINC2895765	0.500	223.3 Da LogP 0.57 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCCC(=O)NCCS(=O)(=O)O`
ZINC39317991	0.500	290.4 Da LogP 0.34 TPSA 118.0	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCOCCCCS(=O)(=O)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.