Protein profile

KP13_02527

Phenolic acid decarboxylase subunit C

Genome: KpKP13

Gene: AHE42991.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GS97

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Amino acids 475

Annotations 7

Features 14

PDB binders 3

Druggability 0.778

Overview

Basic information about this protein and its source genome.

Accession: KP13_02527
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42991.1
Status: annotated
Amino acids: 475
Structure source: AlphaFold + ColabFold

4.1.1.-

GO:0016831 Catalysis of the nonhydrolytic addition or removal of a carboxyl group to or from a compound. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0008694 Catalysis of the reaction: a 4-hydroxy-3-(all-trans-polyprenyl)benzoate + H+ = a 2-(all-trans-polyprenyl)phenol + CO2. GO:0046872 Binding to a metal ion. GO:0009636 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a toxic stimulus. GO:0006744 The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.

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: Cytoplasmic
ColabFold pLDDT: 95.58

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 0.778

Structure A0A0H3GS97

Pocket Pocket 19

P2Rank 0.923

Structure A0A0H3GS97

Pocket Pocket 1

ColabFold model

FPocket 0.843 · Pocket 13

P2Rank 0.947 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 79 / 4744 genomes with a hit

Normalized 0.017

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

4.1.1.-

Gene Ontology (GO)

GO:0016831 Catalysis of the nonhydrolytic addition or removal of a carboxyl group to or from a compound.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0008694 Catalysis of the reaction: a 4-hydroxy-3-(all-trans-polyprenyl)benzoate + H+ = a 2-(all-trans-polyprenyl)phenol + CO2.
GO:0046872 Binding to a metal ion.
GO:0009636 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a toxic stimulus.
GO:0006744 The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records

Show feature table

Start	End	DB	Term	Name
3	309	SUPERFAMILY	SSF50475	FMN-binding split barrel
464	475	Coils	Coil	Coil
6	441	NCBIfam	TIGR00148	UbiD family decarboxylase
6	441	InterPro	IPR002830	UbiD decarboxylyase family
1	472	PANTHER	PTHR30108	3-OCTAPRENYL-4-HYDROXYBENZOATE CARBOXY-LYASE-RELATED
1	472	InterPro	IPR002830	UbiD decarboxylyase family
4	469	NCBIfam	NF041204	non-oxidative hydroxyarylic acid decarboxylases subunit C
312	467	SUPERFAMILY	SSF143968	UbiD C-terminal domain-like
326	439	Gene3D	G3DSA:3.40.1670.10	-
1	472	Hamap	MF_01985	Phenolic acid decarboxylase.
1	472	InterPro	IPR032902	Phenolic acid decarboxylase subunit C
10	416	Pfam	PF01977	3-octaprenyl-4-hydroxybenzoate carboxy-lyase
10	416	InterPro	IPR002830	UbiD decarboxylyase family
326	439	FunFam	G3DSA:3.40.1670.10:FF:000003	Phenolic acid decarboxylase

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_A0A0H3GS97	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02527	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
19				0.778

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	20.98	0.864
2	1.58	0.024
3	1.19	0.01
4	1.17	0.01
5	1.04	0.006

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
13				0.843

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	25.18	0.904
2	3.77	0.145
3	1.3	0.014
4	0.94	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.

40 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
4LU	6H6X	A5D4Z9	525.5 Da LogP -0.09 TPSA 199.4	2 viol.	✓ Clean	`Cc1cc2c3c(c1C)C(CC=[N+]3C4=C(N2C[C@@H]([C@@H]([…`
7D9	5M1E	P0AAB5	606.5 Da LogP -0.64 TPSA 254.0	3 viol.	✓ Clean	`Cc1cc2c3c(c1C)C(C[C@H](N3C4=C(N2C[C@@H]([C@@H](…`
9JE	5O3M	A6T7M3	104.1 Da LogP 0.14 TPSA 40.5	✓ Ro5	✓ Clean	`C(CCO)CCO`

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
ZINC14771652	1.000	216.4 Da LogP 3.26 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCO`
ZINC15269439	1.000	272.5 Da LogP 4.82 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCCCCCO`
ZINC1574339	1.000	202.3 Da LogP 2.87 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCO`
ZINC4202510	1.000	230.4 Da LogP 3.65 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCCO`
ZINC4521552	1.000	258.4 Da LogP 4.43 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCCCCO`
ZINC4600152	1.000	244.4 Da LogP 4.04 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCCCCCCCCO`
ZINC1644076	0.615	214.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCO`
ZINC1680803	0.615	200.4 Da LogP 4.29 TPSA 20.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCO`
ZINC2385445	0.615	201.4 Da LogP 2.84 TPSA 46.2	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCO`
ZINC34196183	0.615	229.4 Da LogP 3.62 TPSA 46.2	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCO`
ZINC4501366	0.615	204.4 Da LogP 3.42 TPSA 20.2	✓ Ro5	✓ Clean	`OCCCCCCCCCCCS`
ZINC139618309	0.571	301.5 Da LogP 4.02 TPSA 52.5	✓ Ro5	✓ Clean	`OCCCCCCCCCNCCCCCCCCCO`
ZINC247757772	0.571	254.4 Da LogP 3.66 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCC#CCCCCCCCO`
ZINC261828216	0.571	282.5 Da LogP 4.44 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCCC#CCCCCCCCCO`
ZINC26897398	0.571	206.4 Da LogP 2.04 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCSCCCCCO`
ZINC36468523	0.571	256.4 Da LogP 4.21 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCC/C=C\CCCCCCCO`
ZINC62240763	0.571	284.5 Da LogP 4.99 TPSA 40.5	✓ Ro5	✓ Clean	`OCCCCCCCC/C=C\CCCCCCCCO`
ZINC98090187	0.571	217.4 Da LogP 1.68 TPSA 52.5	✓ Ro5	✓ Clean	`OCCCCCCNCCCCCCO`
ZINC113216117	0.500	306.4 Da LogP 2.14 TPSA 68.2	✓ Ro5	✓ Clean	`OCCCCOCCCCOCCCCOCCCCO`
ZINC137540565	0.500	378.6 Da LogP 2.94 TPSA 77.4	✓ Ro5	✓ Clean	`OCCCCOCCCCOCCCCOCCCCOCCCCO`
ZINC14510370	0.500	244.4 Da LogP 3.74 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCO`
ZINC148125630	0.500	201.4 Da LogP 2.71 TPSA 32.3	✓ Ro5	✓ Clean	`CNCCCCCCCCCCCO`
ZINC1531061	0.500	216.3 Da LogP 2.96 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCO`
ZINC1610426	0.500	230.3 Da LogP 3.35 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCO`
ZINC169795588	0.500	240.3 Da LogP 4.44 TPSA 20.2	✓ Ro5	✓ Clean	`OCCCCCCCCCCCC(F)(F)F`
ZINC2012426	0.500	200.4 Da LogP 4.15 TPSA 20.2	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCCO`
ZINC2168567	0.500	202.3 Da LogP 2.57 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCO`
ZINC33966703	0.500	234.3 Da LogP 1.34 TPSA 58.9	✓ Ro5	✓ Clean	`OCCCCOCCCCOCCCCO`
ZINC34564691	0.500	238.4 Da LogP 4.68 TPSA 20.2	✓ Ro5	✓ Clean	`C#CCCCCCCCCCCCCCCO`
ZINC34570000	0.500	226.4 Da LogP 4.85 TPSA 20.2	✓ Ro5	✓ Clean	`C=CCCCCCCCCCCCCCO`
ZINC34586464	0.500	224.4 Da LogP 4.29 TPSA 20.2	✓ Ro5	✓ Clean	`C#CCCCCCCCCCCCCCO`
ZINC3861297	0.500	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCO`
ZINC4284502	0.500	258.4 Da LogP 4.13 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCO`
ZINC44676392	0.500	214.4 Da LogP 4.54 TPSA 20.2	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCCCO`
ZINC5157674	0.500	212.4 Da LogP 4.46 TPSA 20.2	✓ Ro5	✓ Clean	`C=CCCCCCCCCCCCCO`
ZINC5287109	0.500	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCCO`
ZINC95884217	0.500	210.4 Da LogP 3.90 TPSA 20.2	✓ Ro5	✓ Clean	`C#CCCCCCCCCCCCCO`

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.