Protein profile

PA3516

adenylosuccinate lyase

Genome: NC_002516.2

Gene: PA3516 Structure source: AlphaFold UniProt Q9HY93
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Amino acids 483
Annotations 7
Features 26
PDB binders 5
Druggability 0.812

Overview

Basic information about this protein and its source genome.

Accession
PA3516
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3516
Status
annotated
Amino acids
483
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: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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
40.541
Human E-value
1.12e-07
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 0.812
Structure –
Pocket –

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)

1

Gene Ontology (GO)

6
  • 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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records
Show feature table
Start End DB Term Name
400 475 Pfam PF10397 Adenylosuccinate lyase C-terminus
400 475 InterPro IPR019468 Adenylosuccinate lyase C-terminal
42 478 CDD cd01597 pCLME
397 483 Gene3D G3DSA:1.10.40.30 -
397 476 SMART SM00998 ADSL_C_2
397 476 InterPro IPR019468 Adenylosuccinate lyase C-terminal
35 395 Gene3D G3DSA:1.20.200.10 Fumarase/aspartase (Central domain)
35 394 FunFam G3DSA:1.20.200.10:FF:000014 3-carboxy-cis,cis-muconate cycloisomerase
34 479 PANTHER PTHR43172 ADENYLOSUCCINATE LYASE
53 327 Pfam PF00206 Lyase
53 327 InterPro IPR022761 Fumarate lyase, N-terminal
43 480 SUPERFAMILY SSF48557 L-aspartase-like
43 480 InterPro IPR008948 L-Aspartase-like
309 318 ProSitePatterns PS00163 Fumarate lyases signature.
309 318 InterPro IPR020557 Fumarate lyase, conserved site
134 152 PRINTS PR00149 Fumarate lyase superfamily signature
134 152 InterPro IPR000362 Fumarate lyase family
179 197 PRINTS PR00149 Fumarate lyase superfamily signature
179 197 InterPro IPR000362 Fumarate lyase family
309 325 PRINTS PR00149 Fumarate lyase superfamily signature
309 325 InterPro IPR000362 Fumarate lyase family
264 291 PRINTS PR00149 Fumarate lyase superfamily signature
264 291 InterPro IPR000362 Fumarate lyase family
174 194 PRINTS PR00145 Argininosuccinate lyase family signature
264 288 PRINTS PR00145 Argininosuccinate lyase family signature
309 325 PRINTS PR00145 Argininosuccinate lyase family signature

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 PA3516
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
2 0.812

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.