Protein profile

PA1792

UDP-2,3-diacylglucosamine hydrolase

Genome: NC_002516.2

Gene: PA1792 lpxH Structure source: Experimental + AlphaFold UniProt Q9I2V0
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Amino acids 240
Annotations 9
Features 14
PDB binders 2
Druggability 0.641

Overview

Basic information about this protein and its source genome.

Accession
PA1792
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1792 lpxH
Status
annotated
Amino acids
240
Structure source
Experimental + AlphaFold
EC
3.6.1.54
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0019897 The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. GO:0051861 Binding to a glycolipid, any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic group such as an acylglycerol, a sphingoid, a ceramide (N-acylsphingoid) or a prenyl phosphate. GO:0030145 Binding to a manganese ion (Mn). GO:0008758 Catalysis of the reaction: H2O + UDP-2,3-bis(3-hydroxymyristoyl)glucosamine = 2,3-bis(3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP. GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.641
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MSVLFISDLHLEAERPDITRAFLSFLDERARRAEALYILGDFFEAWIGDDGMDAFQRSIAQSLRQVADGGTRIYLMHGNRDFLIGKAFCREAGCTLLPDPSVIDLYGEPVLLMHGDSLCTRDEAYMRLRRWLRNPLTLWVLRHLPLATRHKLARKLRKESRAQTRMKAVDIIDVTPEEVPRVMRGHGVRTLIHGHTHRPAEHPLDIDGQPARRIVLGDWDRQGWALEIDANGHRQAPFPL

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0019897 The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
  • GO:0051861 Binding to a glycolipid, any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic group such as an acylglycerol, a sphingoid, a ceramide (N-acylsphingoid) or a prenyl phosphate.
  • GO:0030145 Binding to a manganese ion (Mn).
  • GO:0008758 Catalysis of the reaction: H2O + UDP-2,3-bis(3-hydroxymyristoyl)glucosamine = 2,3-bis(3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP.
  • GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.
  • GO:0016462 Catalysis of the hydrolysis of a pyrophosphate bond (diphosphate bond) between two phosphate groups.
  • GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records
Show feature table
Start End DB Term Name
1 240 Hamap MF_00575 UDP-2,3-diacylglucosamine hydrolase [lpxH].
1 240 InterPro IPR010138 UDP-2,3-diacylglucosamine hydrolase
2 233 PANTHER PTHR34990 UDP-2,3-DIACYLGLUCOSAMINE HYDROLASE-RELATED
2 233 InterPro IPR043461 UDP-2,3-diacylglucosamine hydrolase LpxH-like
3 233 NCBIfam TIGR01854 UDP-2,3-diacylglucosamine diphosphatase
3 233 InterPro IPR010138 UDP-2,3-diacylglucosamine hydrolase
1 167 FunFam G3DSA:3.60.21.10:FF:000012 UDP-2,3-diacylglucosamine hydrolase
1 199 Pfam PF00149 Calcineurin-like phosphoesterase
1 199 InterPro IPR004843 Calcineurin-like phosphoesterase domain, ApaH type
4 219 CDD cd07398 MPP_YbbF-LpxH
1 206 Gene3D G3DSA:3.60.21.10 -
1 206 InterPro IPR029052 Metallo-dependent phosphatase-like
1 224 SUPERFAMILY SSF56300 Metallo-dependent phosphatases
1 224 InterPro IPR029052 Metallo-dependent phosphatase-like

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

5 + 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 5B4B
X-ray 1.60 Å A,B
100.0% 1-240
PDBe RCSB PDBj File
Viewing
PDB 5B49
X-ray 1.65 Å A,B
100.0% 1-240
PDBe RCSB PDBj File
Loaded
PDB 5B4A
X-ray 1.72 Å A,B
100.0% 1-240
PDBe RCSB PDBj File
Loaded
PDB 5B4D
X-ray 1.75 Å A,B
100.0% 1-240
PDBe RCSB PDBj File
Loaded
PDB 5B4C
X-ray 1.96 Å A,B
100.0% 1-240
PDBe RCSB PDBj File
Loaded
AlphaFold PA1792
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 0.641

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 31.96 0.941
2 5.9 0.289
3 5.14 0.237
4 2.74 0.083
5 0.7 0.001

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.

52 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
LP5
6PH9
A6T5R0 711.9 Da LogP 4.91 TPSA 212.3 2 viol. ✓ Clean CCCCCCCCCCC[C@H](CC(=O)N[C@@H]1[C@H]([C@@H]([C@…
OKV
6PIB
A6T5R0 453.5 Da LogP 3.13 TPSA 60.9 ✓ Ro5 ✓ Clean CC(=O)N1CCc2c1ccc(c2)S(=O)(=O)N3CCN(CC3)c4cccc(…

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.