Protein profile

PA3970

AMP nucleosidase

Genome: NC_002516.2

Gene: amn PA3970 Structure source: AlphaFold UniProt Q9HX46
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Amino acids 499
Annotations 6
Features 16
PDB binders 1
Druggability 0.712

Overview

Basic information about this protein and its source genome.

Accession
PA3970
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
amn PA3970
Status
annotated
Amino acids
499
Structure source
AlphaFold
EC
3.2.2.4
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:0008714 Catalysis of the reaction: AMP + H2O = D-ribose 5-phosphate + adenine. GO:0044209 The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from derivatives of it (either adenine, ADP or adenosine 3',5'-bisphosphate) without de novo synthesis. GO:0009116 The chemical reactions and pathways involving a nucleoside, a nucleobase linked to either beta-D-ribofuranose (a ribonucleoside) or 2-deoxy-beta-D-ribofuranose, (a deoxyribonucleoside), e.g. adenosine, guanosine, inosine, cytidine, uridine and deoxyadenosine, deoxyguanosine, deoxycytidine and thymidine (= deoxythymidine). 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
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 0.712
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

5
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0008714 Catalysis of the reaction: AMP + H2O = D-ribose 5-phosphate + adenine.
  • GO:0044209 The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from derivatives of it (either adenine, ADP or adenosine 3',5'-bisphosphate) without de novo synthesis.
  • GO:0009116 The chemical reactions and pathways involving a nucleoside, a nucleobase linked to either beta-D-ribofuranose (a ribonucleoside) or 2-deoxy-beta-D-ribofuranose, (a deoxyribonucleoside), e.g. adenosine, guanosine, inosine, cytidine, uridine and deoxyadenosine, deoxyguanosine, deoxycytidine and thymidine (= deoxythymidine).
  • 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.

16 records
Show feature table
Start End DB Term Name
284 467 Pfam PF01048 Phosphorylase superfamily
284 467 InterPro IPR000845 Nucleoside phosphorylase domain
25 179 Pfam PF10423 Bacterial AMP nucleoside phosphorylase N-terminus
25 179 InterPro IPR018953 AMP nucleoside phosphorylase, N-terminal
16 499 Hamap MF_01932 AMP nucleosidase [amn].
16 499 InterPro IPR011271 AMP nucleosidase
189 475 PANTHER PTHR43691 URIDINE PHOSPHORYLASE
23 43 Coils Coil Coil
187 499 Gene3D G3DSA:3.40.50.1580 Nucleoside phosphorylase domain
187 499 InterPro IPR035994 Nucleoside phosphorylase superfamily
24 499 NCBIfam TIGR01717 AMP nucleosidase
24 499 InterPro IPR011271 AMP nucleosidase
18 186 Gene3D G3DSA:3.30.1730.10 -
18 186 InterPro IPR037109 AMP nucleoside phosphorylase, N-terminal domain superfamily
22 499 SUPERFAMILY SSF53167 Purine and uridine phosphorylases
22 499 InterPro IPR035994 Nucleoside phosphorylase superfamily

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 PA3970
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
3 0.712
5 0.345

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.

32 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
FMP
1T8S
P0AE12 347.2 Da LogP -1.79 TPSA 196.9 1 viol. ✓ Clean c1nc2c(c(n1)N)[nH]nc2[C@H]3[C@@H]([C@@H]([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.