Protein profile

PA1521

guanine deaminase

Genome: NC_002516.2

Gene: PA1521 Structure source: AlphaFold UniProt Q9I3J2
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Amino acids 434
Annotations 8
Features 15
PDB binders 3
Druggability 0.344

Overview

Basic information about this protein and its source genome.

Accession
PA1521
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1521
Status
annotated
Amino acids
434
Structure source
AlphaFold
EC
3.5.4.3
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:0008892 Catalysis of the reaction: guanine + H2O + H+ = xanthine + NH4+. GO:0008270 Binding to a zinc ion (Zn). GO:0006147 The chemical reactions and pathways resulting in the breakdown of guanine, 2-amino-6-hydroxypurine, a purine that is one of the five main bases found in nucleic acids and a component of a number of phosphorylated guanosine derivatives whose metabolic or regulatory functions are important. GO:0046098 The chemical reactions and pathways involving guanine, 2-amino-6-hydroxypurine, a purine that is one of the five main bases found in nucleic acids and a component of a number of phosphorylated guanosine derivatives whose metabolic or regulatory functions are important. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
37.795
Human E-value
1.36e-20
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 0.344
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0008892 Catalysis of the reaction: guanine + H2O + H+ = xanthine + NH4+.
  • GO:0008270 Binding to a zinc ion (Zn).
  • GO:0006147 The chemical reactions and pathways resulting in the breakdown of guanine, 2-amino-6-hydroxypurine, a purine that is one of the five main bases found in nucleic acids and a component of a number of phosphorylated guanosine derivatives whose metabolic or regulatory functions are important.
  • GO:0046098 The chemical reactions and pathways involving guanine, 2-amino-6-hydroxypurine, a purine that is one of the five main bases found in nucleic acids and a component of a number of phosphorylated guanosine derivatives whose metabolic or regulatory functions are important.
  • GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
  • GO:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records
Show feature table
Start End DB Term Name
29 88 SUPERFAMILY SSF51338 Composite domain of metallo-dependent hydrolases
29 88 InterPro IPR011059 Metal-dependent hydrolase, composite domain superfamily
9 424 Gene3D G3DSA:2.30.40.10 Urease, subunit C, domain 1
9 424 InterPro IPR011059 Metal-dependent hydrolase, composite domain superfamily
71 374 SUPERFAMILY SSF51556 Metallo-dependent hydrolases
71 374 InterPro IPR032466 Metal-dependent hydrolase
28 427 NCBIfam TIGR02967 guanine deaminase
28 427 InterPro IPR014311 Guanine deaminase
8 427 CDD cd01303 GDEase
8 427 InterPro IPR014311 Guanine deaminase
69 430 Pfam PF01979 Amidohydrolase family
69 430 InterPro IPR006680 Amidohydrolase-related
72 390 Gene3D G3DSA:3.20.20.140 -
72 373 FunFam G3DSA:3.20.20.140:FF:000022 Guanine deaminase
3 433 PANTHER PTHR11271 GUANINE DEAMINASE

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 PA1521
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
5 0.344
4 0.322
2 0.267

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
GUN
2OOD
Q89NG0 151.1 Da LogP -0.77 TPSA 100.5 ✓ Ro5 ✓ Clean c1[nH]c2c(n1)C(=O)NC(=N2)N
TXC
4AQL
Q9Y2T3 324.3 Da LogP -0.80 TPSA 151.1 ✓ Ro5 ✓ Clean CC(C)[C@@H](C(=O)OCCOCn1cnc2c1N=C(NC2=O)N)N
XAN
6OHA
Q07729 152.1 Da LogP -1.06 TPSA 94.4 ✓ Ro5 ✓ Clean c1[nH]c2c(n1)C(=O)NC(=O)N2

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.