Protein profile

PA3517

adenylosuccinate lyase

Genome: NC_002516.2

Gene: PA3517 Structure source: AlphaFold UniProt Q9HY92
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Amino acids 477
Annotations 9
Features 31
PDB binders 5
Druggability 0.953

Overview

Basic information about this protein and its source genome.

Accession
PA3517
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3517
Status
annotated
Amino acids
477
Structure source
AlphaFold
EC
5.5.1.2
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:0070626 Catalysis of the reaction: (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. GO:0047472 Catalysis of the reaction: 2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate = 3-carboxy-cis,cis-muconate + H+. GO:0004018 Catalysis of the reaction: N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP. GO:0044208 The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from inosine 5'-monophosphate (IMP). GO:0006189 The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
25.607
Human E-value
1.16e-24
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 0.953
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0070626 Catalysis of the reaction: (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
  • GO:0047472 Catalysis of the reaction: 2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate = 3-carboxy-cis,cis-muconate + H+.
  • GO:0004018 Catalysis of the reaction: N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
  • GO:0044208 The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from inosine 5'-monophosphate (IMP).
  • GO:0006189 The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
  • 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:0009152 The chemical reactions and pathways resulting in the formation of a purine ribonucleotide, a compound consisting of ribonucleoside (a purine base linked to a ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

Sequence Features

Domain/signature hits from InterPro and related databases.

31 records
Show feature table
Start End DB Term Name
10 447 CDD cd01597 pCLME
446 477 MobiDBLite mobidb-lite consensus disorder prediction
277 293 PRINTS PR00145 Argininosuccinate lyase family signature
232 256 PRINTS PR00145 Argininosuccinate lyase family signature
101 123 PRINTS PR00145 Argininosuccinate lyase family signature
142 162 PRINTS PR00145 Argininosuccinate lyase family signature
366 445 SMART SM00998 ADSL_C_2
366 445 InterPro IPR019468 Adenylosuccinate lyase C-terminal
457 471 MobiDBLite mobidb-lite consensus disorder prediction
3 363 FunFam G3DSA:1.20.200.10:FF:000014 3-carboxy-cis,cis-muconate cycloisomerase
277 293 PRINTS PR00149 Fumarate lyase superfamily signature
277 293 InterPro IPR000362 Fumarate lyase family
232 259 PRINTS PR00149 Fumarate lyase superfamily signature
232 259 InterPro IPR000362 Fumarate lyase family
147 165 PRINTS PR00149 Fumarate lyase superfamily signature
147 165 InterPro IPR000362 Fumarate lyase family
102 120 PRINTS PR00149 Fumarate lyase superfamily signature
102 120 InterPro IPR000362 Fumarate lyase family
2 450 PANTHER PTHR43172 ADENYLOSUCCINATE LYASE
366 450 Gene3D G3DSA:1.10.40.30 -
15 444 NCBIfam TIGR00928 adenylosuccinate lyase
15 444 InterPro IPR004769 Adenylosuccinate lyase
11 445 SUPERFAMILY SSF48557 L-aspartase-like
11 445 InterPro IPR008948 L-Aspartase-like
277 286 ProSitePatterns PS00163 Fumarate lyases signature.
277 286 InterPro IPR020557 Fumarate lyase, conserved site
3 363 Gene3D G3DSA:1.20.200.10 Fumarase/aspartase (Central domain)
367 442 Pfam PF10397 Adenylosuccinate lyase C-terminus
367 442 InterPro IPR019468 Adenylosuccinate lyase C-terminal
17 298 Pfam PF00206 Lyase
17 298 InterPro IPR022761 Fumarate lyase, N-terminal

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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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 PA3517
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
8 0.873
6 0.352
5 0.305
12 0.202

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.

55 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
DTT
1RE5
Q88N37 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CS)O)O)S
FUM
5XNZ
A0A0K2JL82 116.1 Da LogP -0.29 TPSA 74.6 ✓ Ro5 ✓ Clean C(=C/C(=O)O)\C(=O)O
MLI
2PFM
A0A6L8PR48 102.0 Da LogP -3.12 TPSA 80.3 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(=O)[O-]
OXL
2X75
Q7A0G9 88.0 Da LogP -3.51 TPSA 80.3 ✓ Ro5 ✓ Clean C(=O)(C(=O)[O-])[O-]
SIN
4EEI
Q5NIQ1 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=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.