Protein profile

PA3863

FAD-dependent catabolic D-arginine dehydrogenase DauA

Genome: NC_002516.2

Gene: PA3863 dauA Structure source: Experimental + AlphaFold UniProt Q9HXE3
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Amino acids 375
Annotations 7
Features 8
PDB binders 6
Druggability 0.458

Overview

Basic information about this protein and its source genome.

Accession
PA3863
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3863 dauA
Status
annotated
Amino acids
375
Structure source
Experimental + AlphaFold
EC
1.4.99.6
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0008718 Catalysis of the reaction: a D-alpha-amino acid + a quinone + H2O = a 2-oxocarboxylate + a quinol + NH4+. GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. GO:0006525 The chemical reactions and pathways involving arginine, 2-amino-5-(carbamimidamido)pentanoic acid. GO:0006527 The chemical reactions and pathways resulting in the breakdown of L-arginine. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
25.466
Human E-value
3.46e-08
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 0.458
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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0008718 Catalysis of the reaction: a D-alpha-amino acid + a quinone + H2O = a 2-oxocarboxylate + a quinol + NH4+.
  • GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
  • GO:0006525 The chemical reactions and pathways involving arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
  • GO:0006527 The chemical reactions and pathways resulting in the breakdown of L-arginine.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Sequence Features

Domain/signature hits from InterPro and related databases.

8 records
Show feature table
Start End DB Term Name
5 347 Pfam PF01266 FAD dependent oxidoreductase
5 347 InterPro IPR006076 FAD dependent oxidoreductase
3 358 PANTHER PTHR13847 SARCOSINE DEHYDROGENASE-RELATED
4 357 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
4 357 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
84 308 Gene3D G3DSA:3.30.9.10 -
5 348 Gene3D G3DSA:3.50.50.60 -
5 348 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily

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

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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 7RDF
X-ray 1.29 Å A
100.0% 1-375
PDBe RCSB PDBj File
Viewing
PDB 6P9D
X-ray 1.33 Å A
100.0% 1-375
PDBe RCSB PDBj File
Loaded
PDB 6PLD
X-ray 1.55 Å A
100.0% 1-375
PDBe RCSB PDBj File
Loaded
PDB 3NYC
X-ray 1.06 Å A
99.7% 2-375
PDBe RCSB PDBj File
Loaded
PDB 3SM8
X-ray 1.07 Å A
99.7% 2-375
PDBe RCSB PDBj File
Loaded
PDB 3NYE
X-ray 1.30 Å A
99.7% 2-375
PDBe RCSB PDBj File
Loaded
PDB 3NYF
X-ray 1.30 Å A
99.7% 2-375
PDBe RCSB PDBj File
Loaded
AlphaFold PA3863
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.

56 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
6FA
6PLD 1.55 Å Open crystal
801.6 Da LogP -2.72 TPSA 383.2 3 viol. ✓ Clean Cc1cc2c(c(c1C)O)N=C3C(=O)NC(=O)N=C3N2C[C@@H]([C…
FDA
6P9D 1.33 Å Open crystal
787.6 Da LogP -1.75 TPSA 363.3 3 viol. ✓ Clean Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…
FNK
3SM8 1.07 Å Open crystal
871.7 Da LogP -0.78 TPSA 371.6 3 viol. ✓ Clean Cc1cc2c(cc1C)N(C3=C(N2C[C@@H]([C@@H]([C@@H](CO[…
HHI
3NYF 1.30 Å Open crystal
153.1 Da LogP 0.06 TPSA 89.8 ✓ Ro5 ✓ Clean [H]/N=C(/Cc1cnc[nH]1)\C(=O)O
IAR
3NYC 1.06 Å Open crystal
172.2 Da LogP -0.65 TPSA 123.0 ✓ Ro5 ✓ Clean [H]/N=C(\CCCN/C(=N/[H])/N)/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.