Protein profile

PA3774

acetylpolyamine aminohydrolase

Genome: NC_002516.2

Gene: PA3774 Structure source: Experimental + AlphaFold UniProt Q9HXM1
Export view
Amino acids 380
Annotations 5
Features 14
PDB binders 36
Druggability 0.576

Overview

Basic information about this protein and its source genome.

Accession
PA3774
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3774
Status
annotated
Amino acids
380
Structure source
Experimental + AlphaFold
EC
3.5.1.-
GO
GO:0004407 Removal of an acetyl group from a lysine residue in a histone. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. GO:0046872 Binding to a metal ion. GO:0040029 A process that modulates the frequency, rate or extent of gene expression through chromatin remodeling either by modifying higher order chromatin fiber structure, nucleosomal histones, or cytosine methylation of DNA. Once established, this regulation may be maintained over many cell divisions. It can also be heritable in the absence of the instigating signal.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
38.117
Human E-value
1.2500000000000001e-29
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 0.576
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

4
  • GO:0004407 Removal of an acetyl group from a lysine residue in a histone.
  • GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
  • GO:0046872 Binding to a metal ion.
  • GO:0040029 A process that modulates the frequency, rate or extent of gene expression through chromatin remodeling either by modifying higher order chromatin fiber structure, nucleosomal histones, or cytosine methylation of DNA. Once established, this regulation may be maintained over many cell divisions. It can also be heritable in the absence of the instigating signal.

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records
Show feature table
Start End DB Term Name
5 366 CDD cd09996 HDAC_classII_1
28 329 PANTHER PTHR48252 HISTONE DEACETYLASE 2-RELATED
2 355 SUPERFAMILY SSF52768 Arginase/deacetylase
2 355 InterPro IPR023696 Ureohydrolase domain superfamily
2 380 Gene3D G3DSA:3.40.800.20 Histone deacetylase domain
2 380 InterPro IPR037138 Histone deacetylase domain superfamily
140 163 PRINTS PR01270 Histone deacetylase superfamily signature
140 163 InterPro IPR000286 Histone deacetylase family
259 269 PRINTS PR01270 Histone deacetylase superfamily signature
259 269 InterPro IPR000286 Histone deacetylase family
174 189 PRINTS PR01270 Histone deacetylase superfamily signature
174 189 InterPro IPR000286 Histone deacetylase family
39 326 Pfam PF00850 Histone deacetylase domain
39 326 InterPro IPR023801 Histone deacetylase domain

3D Structure

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

3D visualization script Full viewer

Loading 3D structure...

Legend High Medium Low

Structural evidence

7 + 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 5LI3
X-ray 2.40 Å A,B
100.0% 1-380
PDBe RCSB PDBj File
Viewing
PDB 5G0X
X-ray 1.70 Å A,C
99.7% 2-380
PDBe RCSB PDBj File
Loaded
PDB 5G10
X-ray 1.71 Å A,B
99.7% 2-380
PDBe RCSB PDBj File
Loaded
PDB 5G13
X-ray 1.99 Å A,B
99.7% 2-380
PDBe RCSB PDBj File
Loaded
PDB 5G12
X-ray 2.02 Å A,B
99.7% 2-380
PDBe RCSB PDBj File
Loaded
PDB 5G0Y
X-ray 2.29 Å A,B
99.7% 2-380
PDBe RCSB PDBj File
Loaded
PDB 5G11
X-ray 2.48 Å A,B
99.7% 2-380
PDBe RCSB PDBj File
Loaded
AlphaFold PA3774
AlphaFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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.

186 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

Show only:
Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
6DK
5G10 1.71 Å Open crystal
319.3 Da LogP 3.21 TPSA 69.6 ✓ Ro5 ✓ Clean c1ccc(cc1)NC(=O)CCCCCCC(C(F)(F)F)(O)O
7H1
5G11 2.48 Å Open crystal
480.2 Da LogP 3.94 TPSA 78.4 ✓ Ro5 ✓ Clean c1ccc(cc1)NC(=O)C(C(C(C(C(C(C(=O)NO)(F)F)(F)F)(…
9RB
5LI3 2.40 Å Open crystal
299.3 Da LogP 2.97 TPSA 91.9 ✓ Ro5 Alert Cc1c(c(n(n1)C)C)/N=N/c2ccc(cc2)/C=C/C(=O)NO

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.