Protein profile

PA4024

ethanolamine ammonia-lyase large subunit

Genome: NC_002516.2

Gene: eutB PA4024 Structure source: AlphaFold UniProt Q9HX03

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Amino acids 464

Annotations 8

Features 17

PDB binders 4

Druggability 0.738

Overview

Basic information about this protein and its source genome.

Accession: PA4024
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: eutB PA4024
Status: annotated
Amino acids: 464
Structure source: AlphaFold

4.3.1.7

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0009350 An enzyme complex that catalyzes the breakdown of ethanolamine to form acetaldehyde and ammonia. GO:0031471 An organelle found in bacteria consisting of a proteinaceous coat containing enzymes for the degradation of ethanolamine whose purpose is the protection of the rest of the cell from the toxic acetaldehyde product of the enzyme ethanolamine ammonia lyase. GO:0031419 Binding to cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. GO:0008851 Catalysis of the reaction: ethanolamine = acetaldehyde + NH4+. GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Cytoplasmic

Selected Druggability evidence

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 0.738

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MARFTHSVGGETYRFDSLKDVMAKASPARSGDFLAGVAASNDGERVAAQMALADIPLKHFLDEALIPYEDDEVTRLIIDTHQRDAFAPVSHLTVGGFRDWLLGDAADEASLRALAPGLTPEMAAAVSKIMRVQDLVLVAQKIRVVTRFRNTLGLRGRLSTRLQPNHPTDDPAGIAASILDGLLFGNGDAMLGINPATDSMASICALLEMLDAIIQRYEIPTQACVLTHVTSSIEAINRGVPLDLVFQSIAGTEAANASFGISLKILQEGYEAGLSQKRGTLGNNLMYFETGQGSALSANAHHGVDQQTCETRAYAVARHFKPFLVNTVVGFIGPEYLYNGKQIIRAGLEDHFCGKLLGVPMGCDICYTNHAEADQDDMDMLLTLLGVAGINFIMGIPGSDDVMLNYQTTSFHDALYARQTLGLKPAPEFEDWLQRMGIFTQADGRIRFGDELPPAFRQALAQLA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

4.3.1.7

Gene Ontology (GO)

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0009350 An enzyme complex that catalyzes the breakdown of ethanolamine to form acetaldehyde and ammonia.
GO:0031471 An organelle found in bacteria consisting of a proteinaceous coat containing enzymes for the degradation of ethanolamine whose purpose is the protection of the rest of the cell from the toxic acetaldehyde product of the enzyme ethanolamine ammonia lyase.
GO:0031419 Binding to cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
GO:0008851 Catalysis of the reaction: ethanolamine = acetaldehyde + NH4+.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
GO:0046336 The chemical reactions and pathways resulting in the breakdown of ethanolamine (2-aminoethanol), an important water-soluble base of phospholipid (phosphatidylethanolamine).

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
3	457	Hamap	MF_00861	Ethanolamine ammonia-lyase large subunit [eutB].
3	457	InterPro	IPR010628	Ethanolamine ammonia-lyase heavy chain
3	55	Gene3D	G3DSA:2.30.170.30	-
3	55	InterPro	IPR044941	Ethanolamine ammonia-lyase heavy chain, N-terminal domain
3	55	FunFam	G3DSA:2.30.170.30:FF:000002	Ethanolamine ammonia-lyase large subunit
143	454	FunFam	G3DSA:3.20.20.70:FF:000055	Ethanolamine ammonia-lyase heavy chain
143	453	Gene3D	G3DSA:3.20.20.70	Aldolase class I
143	453	InterPro	IPR013785	Aldolase-type TIM barrel
56	142	FunFam	G3DSA:1.10.220.70:FF:000002	Ethanolamine ammonia-lyase large subunit
4	457	PANTHER	PTHR39329	ETHANOLAMINE AMMONIA-LYASE HEAVY CHAIN
4	457	InterPro	IPR010628	Ethanolamine ammonia-lyase heavy chain
56	142	Gene3D	G3DSA:1.10.220.70	lyase
56	142	InterPro	IPR044939	Ethanolamine ammonia-lyase heavy chain, domain 2
13	441	Pfam	PF06751	Ethanolamine ammonia lyase large subunit (EutB)
13	441	InterPro	IPR010628	Ethanolamine ammonia-lyase heavy chain
2	461	PIRSF	PIRSF018788	EutB
2	461	InterPro	IPR010628	Ethanolamine ammonia-lyase heavy chain

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 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA4024	AlphaFold	—	—	full sequence	—	Viewing

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
6				0.738

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.

54 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
2A1	3ABQ	P0AEJ6	75.1 Da LogP -0.67 TPSA 46.2	✓ Ro5	✓ Clean	`C[C@@H](CO)N`
2A3	3ANY	P0AEJ6	75.1 Da LogP -0.67 TPSA 46.2	✓ Ro5	✓ Clean	`C[C@H](CO)N`
5AD	5YSN	P0AEJ6	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O`
ETA	3ABO	P0AEJ6	61.1 Da LogP -1.06 TPSA 46.2	✓ Ro5	✓ Clean	`C(CO)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).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC100352250	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]1O`
ZINC1095430	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]1O`
ZINC13542750	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H]…`
ZINC135734	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H]1O`
ZINC17005625	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]1O`
ZINC1999286	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]1O`
ZINC3869309	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H]1O`
ZINC3869310	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H]…`
ZINC3869311	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H]…`
ZINC3869312	1.000	251.2 Da LogP -0.95 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H…`
ZINC1702626	0.974	281.3 Da LogP -1.59 TPSA 139.5	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H]…`
ZINC4821676	0.974	281.3 Da LogP -1.59 TPSA 139.5	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H…`
ZINC4821679	0.974	281.3 Da LogP -1.59 TPSA 139.5	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H]…`
ZINC4821682	0.974	281.3 Da LogP -1.59 TPSA 139.5	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H…`
ZINC5139067	0.721	283.3 Da LogP -1.04 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CS)[C@@H](O)[C@H]1O`
ZINC2047403	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H]1O`
ZINC2047673	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC2169830	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC3201876	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC3201878	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC3814316	0.705	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]…`
ZINC3830178	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3830179	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC3978047	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC3978048	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC3978049	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]1O`
ZINC4048240	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO)[C@@H](O)[C@H]1O`
ZINC4773848	0.705	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H]…`
ZINC4773849	0.705	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H…`
ZINC4773850	0.705	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@H…`
ZINC4773851	0.705	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@…`
ZINC77981211	0.705	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H]…`
ZINC82228511	0.705	266.3 Da LogP -2.01 TPSA 145.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]1O`
ZINC8580514	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H]1O`
ZINC895113	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H]1O`
ZINC896706	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC970363	0.705	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@H]1O`
ZINC1081541	0.689	285.7 Da LogP -0.73 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CCl)[C@@H](O)[C@@H]…`
ZINC4188096	0.689	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188103	0.689	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC4188112	0.689	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO)[C@@H](O)[C@@H](…`
ZINC4188116	0.689	297.3 Da LogP -2.62 TPSA 159.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC5941240	0.689	269.2 Da LogP -1.00 TPSA 119.3	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CF)[C@@H](O)[C@H]1O`
ZINC100349915	0.681	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@@H…`
ZINC105279440	0.681	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]1O`
ZINC12501834	0.681	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@@…`
ZINC25963247	0.681	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H]…`
ZINC3869319	0.681	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H…`
ZINC5929300	0.681	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@H](O)[C@H]…`
ZINC895091	0.681	297.3 Da LogP -0.61 TPSA 119.3	✓ Ro5	✓ Clean	`CSC[C@@H]1O[C@H](n2cnc3c(N)ncnc32)[C@@H](O)[C@H…`

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.