Protein profile

PA5106

N-formimino-L-glutamate deiminase

Genome: NC_002516.2

Gene: PA5106 hutF Structure source: Experimental + AlphaFold UniProt Q9HU77
Export view
Amino acids 453
Annotations 10
Features 13
PDB binders 9
Druggability 0.448

Overview

Basic information about this protein and its source genome.

Accession
PA5106
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5106 hutF
Status
annotated
Amino acids
453
Structure source
Experimental + AlphaFold
EC
3.5.3.13
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:0019239 Catalysis of the removal of an amino group from a substrate, producing a substituted or nonsubstituted ammonia (NH4+/NH2R). GO:0050416 Catalysis of the reaction: N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH4+. GO:0046872 Binding to a metal ion. GO:0006548 The chemical reactions and pathways resulting in the breakdown of L-histidine. GO:0019556 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-histidine into other compounds, including glutamate and formamide.

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 0.448
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0019239 Catalysis of the removal of an amino group from a substrate, producing a substituted or nonsubstituted ammonia (NH4+/NH2R).
  • GO:0050416 Catalysis of the reaction: N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH4+.
  • GO:0046872 Binding to a metal ion.
  • GO:0006548 The chemical reactions and pathways resulting in the breakdown of L-histidine.
  • GO:0019556 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-histidine into other compounds, including glutamate and formamide.
  • GO:0019557 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-histidine into other compounds, including glutamate and formate.
  • 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.

13 records
Show feature table
Start End DB Term Name
19 434 PANTHER PTHR11271 GUANINE DEAMINASE
50 374 SUPERFAMILY SSF51556 Metallo-dependent hydrolases
50 374 InterPro IPR032466 Metal-dependent hydrolase
359 436 SUPERFAMILY SSF51338 Composite domain of metallo-dependent hydrolases
359 436 InterPro IPR011059 Metal-dependent hydrolase, composite domain superfamily
9 426 CDD cd01313 Met_dep_hydrolase_E
1 452 NCBIfam TIGR02022 formimidoylglutamate deiminase
1 452 InterPro IPR010252 Formimidoylglutamate deiminase
6 432 Gene3D G3DSA:2.30.40.10 Urease, subunit C, domain 1
6 432 InterPro IPR011059 Metal-dependent hydrolase, composite domain superfamily
52 438 Gene3D G3DSA:3.20.20.140 -
48 428 Pfam PF01979 Amidohydrolase family
48 428 InterPro IPR006680 Amidohydrolase-related

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

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 3MDU
X-ray 1.40 Å A
100.0% 1-453
PDBe RCSB PDBj File
Viewing
PDB 4RDW
X-ray 1.59 Å A
100.0% 1-453
PDBe RCSB PDBj File
Loaded
PDB 4RZB
X-ray 1.86 Å A,B
100.0% 1-453
PDBe RCSB PDBj File
Loaded
PDB 3MDW
X-ray 1.90 Å A,B,C,D
100.0% 1-453
PDBe RCSB PDBj File
Loaded
PDB 4RDV
X-ray 2.08 Å A,B,C,D
100.0% 1-453
PDBe RCSB PDBj File
Loaded
AlphaFold PA5106
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
5 0.448
1 0.399

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 28.76 0.927
2 3.69 0.14
3 2.56 0.072
4 1.3 0.014
5 1.09 0.007

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.

59 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
NFQ
3MDW 1.90 Å Open crystal
160.1 Da LogP -0.89 TPSA 110.5 ✓ Ro5 ✓ Clean [H]/N=C/N[C@@H](CC(=O)O)C(=O)O
NGQ
3MDU 1.40 Å Open crystal
189.2 Da LogP -1.21 TPSA 136.5 ✓ Ro5 ✓ Clean [H]/N=C(\N)/N[C@@H](CCC(=O)O)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.