Protein profile

KP13_31527

3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase

Genome: KpKP13

Gene: mhpA AHE44128.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GR47

Export view

Amino acids 554

Annotations 5

Features 17

PDB binders 5

Druggability 0.986

Overview

Basic information about this protein and its source genome.

Accession: KP13_31527
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: mhpA AHE44128.1
Status: annotated
Amino acids: 554
Structure source: AlphaFold + ColabFold

1.14.13.127

GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0019622 The chemical reactions and pathways resulting in the breakdown of 3-(3-hydroxy)phenylpropionate, a hydroxylated derivative of phenylpropionate. GO:0008688 Catalysis of the reaction: 3-(3-hydroxyphenyl)propionate + NADH + oxygen + H+ = 3-(2,3-dihydroxyphenyl)propionate + NAD+ + H2O. GO:0019380 The chemical reactions and pathways resulting in the breakdown of 3-phenylpropionate, the anion of phenylpropanoic acid.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 22.917
Human E-value: 3.42e-09
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 86.59

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 0.986

Structure A0A0H3GR47

Pocket Pocket 41

P2Rank 0.94

Structure A0A0H3GR47

Pocket Pocket 1

ColabFold model

FPocket 0.966 · Pocket 35

P2Rank 0.987 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 28 / 4744 genomes with a hit

Normalized 0.006

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1.14.13.127

Gene Ontology (GO)

GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0019622 The chemical reactions and pathways resulting in the breakdown of 3-(3-hydroxy)phenylpropionate, a hydroxylated derivative of phenylpropionate.
GO:0008688 Catalysis of the reaction: 3-(3-hydroxyphenyl)propionate + NADH + oxygen + H+ = 3-(2,3-dihydroxyphenyl)propionate + NAD+ + H2O.
GO:0019380 The chemical reactions and pathways resulting in the breakdown of 3-phenylpropionate, the anion of phenylpropanoic acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
17	388	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
17	388	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
195	276	Gene3D	G3DSA:3.30.70.2450	-
166	181	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
287	302	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
302	318	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
338	354	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
17	39	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
320	338	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
16	352	Pfam	PF01494	FAD binding domain
16	352	InterPro	IPR002938	FAD-binding domain
18	204	FunFam	G3DSA:3.50.50.60:FF:000126	3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase
7	554	Hamap	MF_01652	3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase [mhpA].
7	554	InterPro	IPR023786	3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase
1	529	PANTHER	PTHR43476	3-(3-HYDROXY-PHENYL)PROPIONATE/3-HYDROXYCINNAMIC ACID HYDROXYLASE
18	351	Gene3D	G3DSA:3.50.50.60	-
18	351	InterPro	IPR036188	FAD/NAD(P)-binding 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...

Legend High Medium Low

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_A0A0H3GR47	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_31527	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
41				0.986
2				0.965

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	23.03	0.885
2	21.9	0.875
3	5.16	0.238
4	3.36	0.119
5	3.11	0.105

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
35				0.966

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	43.78	0.971
2	10.25	0.551
3	3.74	0.143
4	2.26	0.056
5	1.11	0.008

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.

37 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
IPH	1FOH	P15245	94.1 Da LogP 1.39 TPSA 20.2	✓ Ro5	✓ Clean	`c1ccc(cc1)O`
PKS	6U0S	W0C4C9	385.5 Da LogP 5.45 TPSA 62.6	1 viol.	✓ Clean	`C/C=C(\C)/[C@@H]([C@H](C)/C=C(\C)/C=C/C/C(=C/Cc…`
RFH	6C7S	Q5YTV5	839.0 Da LogP 3.15 TPSA 248.0	2 viol.	Alert	`Cc1c(c2c(c3c1O[C@](C3=O)(C)O/C=C/[C@@H]([C@@H](…`
RFP	6BRD	F2R776	823.0 Da LogP 4.34 TPSA 220.1	3 viol.	Alert	`Cc1c(c2c3c4c1O[C@@](C4=O)(O\C=C\[C@@H]([C@H]([C…`
VAK	3IHG	Q54530	412.4 Da LogP 1.71 TPSA 141.4	✓ Ro5	Alert	`CC[C@]1(C[C@@H](c2c(cc3c(c2O)C(=O)c4c(cccc4O)C3…`

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
ZINC4654750	1.000	412.4 Da LogP 1.71 TPSA 141.4	✓ Ro5	Alert	`CC[C@@]1(O)C[C@H](O)c2c(cc3c(c2O)C(=O)c2c(O)ccc…`
ZINC2112807199	0.875	412.4 Da LogP 1.71 TPSA 141.4	✓ Ro5	Alert	`CC[C@]1(O)C[C@@H](O)c2cc3c(c(O)c2[C@H]1C(=O)OC)…`
ZINC2112807200	0.875	412.4 Da LogP 1.71 TPSA 141.4	✓ Ro5	Alert	`CC[C@]1(O)C[C@H](O)c2cc3c(c(O)c2[C@@H]1C(=O)OC)…`
ZINC2112807201	0.875	412.4 Da LogP 1.71 TPSA 141.4	✓ Ro5	Alert	`CC[C@]1(O)C[C@@H](O)c2cc3c(c(O)c2[C@@H]1C(=O)OC…`
ZINC2112807202	0.875	412.4 Da LogP 1.71 TPSA 141.4	✓ Ro5	Alert	`CC[C@]1(O)C[C@H](O)c2cc3c(c(O)c2[C@H]1C(=O)OC)C…`
ZINC102100703	0.836	396.4 Da LogP 2.00 TPSA 121.1	✓ Ro5	Alert	`CC[C@]1(O)C[C@@H](O)c2c(cc3c(c2O)C(=O)c2ccccc2C…`
ZINC102100711	0.836	396.4 Da LogP 2.00 TPSA 121.1	✓ Ro5	Alert	`CC[C@]1(O)C[C@H](O)c2c(cc3c(c2O)C(=O)c2ccccc2C3…`
ZINC6667726	0.836	396.4 Da LogP 2.00 TPSA 121.1	✓ Ro5	Alert	`CC[C@]1(O)C[C@H](O)c2c(cc3c(c2O)C(=O)c2ccccc2C3…`
ZINC6667728	0.836	396.4 Da LogP 2.00 TPSA 121.1	✓ Ro5	Alert	`CC[C@]1(O)C[C@@H](O)c2c(cc3c(c2O)C(=O)c2ccccc2C…`
ZINC3850719	0.789	398.4 Da LogP 1.32 TPSA 141.4	✓ Ro5	Alert	`COC(=O)[C@@H]1c2cc3c(c(O)c2[C@@H](O)C[C@@]1(C)O…`
ZINC5218088	0.772	428.4 Da LogP 1.41 TPSA 161.6	✓ Ro5	Alert	`CC[C@]1(O)C[C@H](O)c2c(O)c3c(c(O)c2[C@@H]1C(=O)…`
ZINC5218089	0.772	428.4 Da LogP 1.41 TPSA 161.6	✓ Ro5	Alert	`CC[C@@]1(O)C[C@H](O)c2c(O)c3c(c(O)c2[C@@H]1C(=O…`
ZINC5218090	0.772	428.4 Da LogP 1.41 TPSA 161.6	✓ Ro5	Alert	`CC[C@]1(O)C[C@@H](O)c2c(O)c3c(c(O)c2[C@@H]1C(=O…`
ZINC5218091	0.772	428.4 Da LogP 1.41 TPSA 161.6	✓ Ro5	Alert	`CC[C@@]1(O)C[C@@H](O)c2c(O)c3c(c(O)c2[C@@H]1C(=…`
ZINC239025564	0.634	695.8 Da LogP 3.63 TPSA 195.0	2 viol.	Alert	`CO[C@@H]1/C=C/O[C@@]2(C)Oc3c(C)c(O)c4c(c3C2=O)C…`
ZINC239025565	0.634	695.8 Da LogP 3.63 TPSA 195.0	2 viol.	Alert	`CO[C@@H]1/C=C/O[C@@]2(C)Oc3c(C)c(O)c4c(c3C2=O)C…`
ZINC239025566	0.634	695.8 Da LogP 3.63 TPSA 195.0	2 viol.	Alert	`CO[C@@H]1/C=C/O[C@@]2(C)Oc3c(C)c(O)c4c(c3C2=O)C…`
ZINC239025567	0.634	695.8 Da LogP 3.63 TPSA 195.0	2 viol.	Alert	`CO[C@@H]1/C=C/O[C@@]2(C)Oc3c(C)c(O)c4c(c3C2=O)C…`
ZINC2048392601	0.587	442.4 Da LogP 0.59 TPSA 178.7	✓ Ro5	Alert	`COC(=O)[C@H]1c2c(O)c3c(c(O)c2[C@H](O)C[C@]1(O)C…`
ZINC239229132	0.571	811.9 Da LogP 3.16 TPSA 217.0	2 viol.	Alert	`CC[C@]1(O)C[C@H](O[C@@H]2C[C@H](N(C)C)[C@H](O[C…`
ZINC239229133	0.571	811.9 Da LogP 3.16 TPSA 217.0	2 viol.	Alert	`CC[C@]1(O)C[C@H](O[C@@H]2C[C@H](N(C)C)[C@H](O[C…`
ZINC239229134	0.571	811.9 Da LogP 3.16 TPSA 217.0	2 viol.	Alert	`CC[C@]1(O)C[C@H](O[C@@H]2C[C@H](N(C)C)[C@H](O[C…`
ZINC113634215	0.526	261.3 Da LogP 4.86 TPSA 23.5	✓ Ro5	✓ Clean	`Oc1ccc(N(c2ccccc2)c2ccccc2)cc1`
ZINC169818837	0.526	352.5 Da LogP 2.77 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1ccc([Si](c2ccccc2)(c2ccccc2)c2ccccc2)cc1`
ZINC1705144	0.526	226.2 Da LogP 2.46 TPSA 54.4	✓ Ro5	Alert	`O=C(C(=O)c1ccc(O)cc1)c1ccccc1`
ZINC3896097	0.526	276.3 Da LogP 4.28 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(C(c2ccccc2)c2ccc(O)cc2)cc1`
ZINC40952767	0.526	277.3 Da LogP 4.57 TPSA 43.7	✓ Ro5	✓ Clean	`Oc1ccc(N(c2ccccc2)c2ccc(O)cc2)cc1`
ZINC5604184	0.526	202.3 Da LogP 3.54 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1ccc(Sc2ccccc2)cc1`
ZINC1679153	0.500	246.3 Da LogP 4.73 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1cccc(-c2ccc(-c3ccccc3)cc2)c1`
ZINC21952721	0.500	200.2 Da LogP 2.47 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc([C@@H](O)c2ccccc2)cc1`
ZINC21952723	0.500	200.2 Da LogP 2.47 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc([C@H](O)c2ccccc2)cc1`
ZINC4253982	0.500	276.3 Da LogP 3.68 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(C(O)(c2ccccc2)c2ccccc2)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.