Protein profile

PA3770

inosine 5'-monophosphate dehydrogenase

Genome: NC_002516.2

Gene: guaB PA3770 Structure source: Experimental + AlphaFold UniProt Q9HXM5
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Amino acids 489
Annotations 10
Features 34
PDB binders 19
Druggability 0.606

Overview

Basic information about this protein and its source genome.

Accession
PA3770
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
guaB PA3770
Status
annotated
Amino acids
489
Structure source
Experimental + AlphaFold
EC
1.1.1.205
GO
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0042802 Binding to an identical protein or proteins. GO:0003938 Catalysis of the reaction: inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+. GO:0046872 Binding to a metal ion. GO:0006177 The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate. GO:0006183 The chemical reactions and pathways resulting in the formation of GTP, guanosine triphosphate.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
52.273
Human E-value
2.7400000000000004e-21
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 0.606
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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0042802 Binding to an identical protein or proteins.
  • GO:0003938 Catalysis of the reaction: inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+.
  • GO:0046872 Binding to a metal ion.
  • GO:0006177 The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.
  • GO:0006183 The chemical reactions and pathways resulting in the formation of GTP, guanosine triphosphate.
  • GO:0006164 The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • 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.

34 records
Show feature table
Start End DB Term Name
1 489 PIRSF PIRSF000130 IMPDH
1 489 InterPro IPR005990 Inosine-5'-monophosphate dehydrogenase
93 148 ProSiteProfiles PS51371 CBS domain profile.
93 148 InterPro IPR000644 CBS domain
2 479 SUPERFAMILY SSF51412 Inosine monophosphate dehydrogenase (IMPDH)
1 488 FunFam G3DSA:3.20.20.70:FF:000003 GMP reductase
294 306 ProSitePatterns PS00487 IMP dehydrogenase / GMP reductase signature.
294 306 InterPro IPR015875 IMP dehydrogenase / GMP reductase, conserved site
157 205 SMART SM00116 cbs_1
157 205 InterPro IPR000644 CBS domain
96 143 SMART SM00116 cbs_1
96 143 InterPro IPR000644 CBS domain
8 456 NCBIfam TIGR01302 IMP dehydrogenase
8 456 InterPro IPR005990 Inosine-5'-monophosphate dehydrogenase
8 464 CDD cd00381 IMPDH
8 464 InterPro IPR001093 IMP dehydrogenase/GMP reductase
94 202 SUPERFAMILY SSF54631 CBS-domain pair
94 202 InterPro IPR046342 CBS domain superfamily
8 475 Pfam PF00478 IMP dehydrogenase / GMP reductase domain
8 475 InterPro IPR001093 IMP dehydrogenase/GMP reductase
8 488 Hamap MF_01964 Inosine-5'-monophosphate dehydrogenase [guaB].
8 488 InterPro IPR005990 Inosine-5'-monophosphate dehydrogenase
2 488 Gene3D G3DSA:3.20.20.70 Aldolase class I
2 488 InterPro IPR013785 Aldolase-type TIM barrel
148 200 Pfam PF00571 CBS domain
148 200 InterPro IPR000644 CBS domain
95 139 Pfam PF00571 CBS domain
95 139 InterPro IPR000644 CBS domain
94 202 CDD cd04601 CBS_pair_IMPDH
5 483 PANTHER PTHR11911 INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED
5 483 InterPro IPR005990 Inosine-5'-monophosphate dehydrogenase
7 475 SMART SM01240 IMPDH_2
152 210 ProSiteProfiles PS51371 CBS domain profile.
152 210 InterPro IPR000644 CBS 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

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Structural evidence

11 + 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 5AHN
X-ray 1.65 Å A
100.0% 1-489
PDBe RCSB PDBj File
Viewing
PDB 5AHM
X-ray 1.74 Å A,B
100.0% 1-489
PDBe RCSB PDBj File
Loaded
PDB 5AHL
X-ray 1.95 Å A
100.0% 1-489
PDBe RCSB PDBj File
Loaded
PDB 6GJV
X-ray 2.11 Å A,B,C,D,E,F,G,H
100.0% 1-489
PDBe RCSB PDBj File
Loaded
PDB 4AVF
X-ray 2.23 Å A,B,C,D
100.0% 1-489
PDBe RCSB PDBj File
Loaded
PDB 3ZFH
X-ray 2.25 Å A
100.0% 1-489
PDBe RCSB PDBj File
Loaded
PDB 4DQW
X-ray 2.51 Å A,B
100.0% 1-489
PDBe RCSB PDBj File
Loaded
PDB 6GK9
X-ray 2.54 Å A,B,C,D,E,F,G,H
100.0% 1-489
PDBe RCSB PDBj File
Loaded
PDB 7QEM
X-ray 3.09 Å A,B,C,D
41.5% 1-203
PDBe RCSB PDBj File
Loaded
PDB 7QBJ
X-ray 2.27 Å A,B,C,D
22.9% 92-203
PDBe RCSB PDBj File
Loaded
PDB 7QDX
X-ray 2.90 Å A,B
22.9% 92-203
PDBe RCSB PDBj File
Loaded
AlphaFold PA3770
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
3 0.606

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 25.21 0.905
2 3.57 0.133
3 2.5 0.069
4 1.72 0.03
5 1.63 0.027

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.

86 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
F2K
6GK9 2.54 Å Open crystal
316.7 Da LogP 0.93 TPSA 124.8 ✓ Ro5 ✓ Clean c1cc(ccc1C2C(=C(OC3=C2C(=O)NC(=O)N3)N)C#N)Cl
IMP
5AHM 1.74 Å Open crystal
348.2 Da LogP -2.15 TPSA 180.0 ✓ Ro5 ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=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.