Protein profile

PA2629

adenylosuccinate lyase

Genome: NC_002516.2

Gene: PA2629 purB Structure source: Experimental + AlphaFold UniProt Q9I0K9
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Amino acids 456
Annotations 10
Features 28
PDB binders 6
Druggability 0.865

Overview

Basic information about this protein and its source genome.

Accession
PA2629
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2629 purB
Status
annotated
Amino acids
456
Structure source
Experimental + AlphaFold
EC
4.3.2.2
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: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:0006163 The chemical reactions and pathways involving a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
24.454
Human E-value
7.34e-06
Gut microbiome off-target
hit
Essential (DEG)
Y
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 0.865
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • 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: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:0006163 The chemical reactions and pathways involving a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
  • 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:0006188 The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate.
  • 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.

28 records
Show feature table
Start End DB Term Name
12 455 NCBIfam TIGR00928 adenylosuccinate lyase
12 455 InterPro IPR004769 Adenylosuccinate lyase
295 304 ProSitePatterns PS00163 Fumarate lyases signature.
295 304 InterPro IPR020557 Fumarate lyase, conserved site
117 135 PRINTS PR00149 Fumarate lyase superfamily signature
117 135 InterPro IPR000362 Fumarate lyase family
252 279 PRINTS PR00149 Fumarate lyase superfamily signature
252 279 InterPro IPR000362 Fumarate lyase family
295 311 PRINTS PR00149 Fumarate lyase superfamily signature
295 311 InterPro IPR000362 Fumarate lyase family
163 181 PRINTS PR00149 Fumarate lyase superfamily signature
163 181 InterPro IPR000362 Fumarate lyase family
383 446 Gene3D G3DSA:1.10.40.30 -
14 313 Pfam PF00206 Lyase
14 313 InterPro IPR022761 Fumarate lyase, N-terminal
23 447 CDD cd01598 PurB
332 446 Pfam PF08328 Adenylosuccinate lyase C-terminal
332 446 InterPro IPR013539 Adenylosuccinate lyase PurB, C-terminal
118 450 Gene3D G3DSA:1.20.200.10 Fumarase/aspartase (Central domain)
1 117 Gene3D G3DSA:1.10.275.10 -
1 117 InterPro IPR024083 Fumarase/histidase, N-terminal
2 456 PANTHER PTHR43411 ADENYLOSUCCINATE LYASE
2 456 InterPro IPR047136 Adenylosuccinate lyase PurB, bacteria
10 455 SUPERFAMILY SSF48557 L-aspartase-like
10 455 InterPro IPR008948 L-Aspartase-like
1 117 FunFam G3DSA:1.10.275.10:FF:000003 Adenylosuccinate lyase
118 385 FunFam G3DSA:1.20.200.10:FF:000004 Adenylosuccinate lyase
383 446 FunFam G3DSA:1.10.40.30:FF:000004 Adenylosuccinate lyase

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

2 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 7T24
X-ray 1.45 Å A
100.0% 1-456
PDBe RCSB PDBj File
Viewing
PDB 7T29
X-ray 1.50 Å A
100.0% 1-456
PDBe RCSB PDBj File
Loaded
AlphaFold PA2629
AlphaFold — — 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
1 0.865
2 0.209

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 Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 4.53 0.194
2 4.37 0.183
3 3.3 0.116
4 2.44 0.066
5 2.3 0.058

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.

56 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
2SA
2PTR
P0AB89 463.3 Da LogP -2.11 TPSA 246.7 2 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
FUM
2PTQ
P0AB89 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-]
N2P
4NSL
Q8ZPZ6 102.2 Da LogP 0.07 TPSA 52.0 ✓ Ro5 ✓ Clean C(CCN)CCN
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.