Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA5413
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: ltaA
Status: annotated
Amino acids: 346
Structure source: ColabFold

GO

GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0006567 The chemical reactions and pathways resulting in the breakdown of L-threonine. GO:0004793 Catalysis of the reaction: L-threonine = glycine + acetaldehyde.

Target profile

Computed evidence for target prioritization.

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

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 0.746

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MTDHTQQFASDNYSGICPEAWAAMAEANRGHERAYGDDQWTARASDYFRQLFETDCEVFFAFNGTAANSLALAALCQSYHSVICSETAHVETDECGAPEFFSNGSKLLLAQTEVGKLTPASIRDIALKRQDIHYPKPRVVTLTQATEVGTVYRPDELKAISATCKELGLHLHMDGARFSNACAFLGCSPAELSWKAGVDVLCFGGTKNGMAVGEAILFFNRDLAEDFDYRCKQAGQLASKMRFLAAPWVGVLQDDAWLRYADHANRCARLLAELVADVPGVSLMFPVEANGVFLQLSEPAIEALRARGWRFYTFIGEGGARFMCSWDTDIERVRELARDIRLVMGA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5

GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0006567 The chemical reactions and pathways resulting in the breakdown of L-threonine.
GO:0004793 Catalysis of the reaction: L-threonine = glycine + acetaldehyde.

Sequence Features

Domain/signature hits from InterPro and related databases.

13 records

Show feature table

Start	End	DB	Term	Name
5	346	PIRSF	PIRSF038940	Low_specificity_LTA
5	346	InterPro	IPR026273	Low specificity L-threonine aldolase, bacteria
4	343	PANTHER	PTHR48097	L-THREONINE ALDOLASE-RELATED
7	341	SUPERFAMILY	SSF53383	PLP-dependent transferases
7	341	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
9	336	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
9	336	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
7	343	CDD	cd06502	TA_like
17	255	Gene3D	G3DSA:3.40.640.10	-
17	255	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
17	255	FunFam	G3DSA:3.40.640.10:FF:000087	L-threonine aldolase
7	297	Pfam	PF01212	Beta-eliminating lyase
7	297	InterPro	IPR001597	Aromatic amino acid beta-eliminating lyase/threonine aldolase

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
ColabFold PA5413	ColabFold	—	—	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
3				0.746
4				0.351
6				0.322
1				0.224

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.

8 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
PLG	3WGB	O07051	306.2 Da LogP -0.12 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNCC(=O)O)O`
PLR	5VYE	A0A166JNM8	233.2 Da LogP 1.01 TPSA 99.9	✓ Ro5	✓ Clean	`Cc1c(cnc(c1O)C)COP(=O)(O)O`
TLP	1LW4	Q9X266	350.3 Da LogP -0.37 TPSA 169.4	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNC(C(C)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).

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
ZINC1656021	1.000	233.2 Da LogP 1.01 TPSA 99.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C)c1O`
ZINC1532708	0.674	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
ZINC1532705	0.652	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC1532514	0.583	247.1 Da LogP 0.52 TPSA 117.0	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C=O)c1O`
ZINC2114966	0.534	332.2 Da LogP 0.99 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(/C=N/CCCC(=O)O)c1O`

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.

PA5413