Protein profile

PA3108

amidophosphoribosyltransferase

Genome: NC_002516.2

Gene: PA3108 purF Structure source: AlphaFold UniProt Q51342
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Amino acids 501
Annotations 7
Features 25
PDB binders 10
Druggability 0.73

Overview

Basic information about this protein and its source genome.

Accession
PA3108
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3108 purF
Status
annotated
Amino acids
501
Structure source
AlphaFold
EC
2.4.2.14
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0004044 Catalysis of the reaction: 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + L-glutamine + H2O. GO:0000287 Binding to a magnesium (Mg) ion. GO:0006189 The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate. GO:0009113 The chemical reactions and pathways resulting in the formation of purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
37.097
Human E-value
2.07e-15
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 0.73
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MCGIVGIVGKSNVNQALYDALTVLQHRGQDAAGIVTCHDDKLYLRKDNGLVRDVFQQRHMQRLIGSVGIGHVRYPTAGSSSSAEAQPFYVNSPYGITLAHNGNLTNVEQLAKEIYESDLRHVNTNSDSEVLLNVFAHELAVRNKLQPTEEDIFAAVSCVHDRCVGGYAVVAMITGHGIVGFRDPNAIRPIVFGQRHTENGVEYMIASESVALDVLGFTLIRDLAPGEAVYITEEGKLYTRQCAKAPKYAPCIFEHVYLARPDSIMDGISVYKARLRMGEKLADKILRERPDHDIDVVIPIPDTSRTAALELANRLGVKFREGFVKNRYIGRTFIMPGQAARKKSVRQKLNAIELEFRGKNVMLVDDSIVRGTTCKQIIQMAREAGAKNVYFCSAAPAVRYPNVYGIDMPSAHELIAHNRSTEDVSKLIGADWLVYQDLPDLIDAVGGGKIKIDHFDCAVFDGEYVTGDVNEAYLNRIEQARNDATKAKSQAVSAIIDLYND

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:0004044 Catalysis of the reaction: 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + L-glutamine + H2O.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:0006189 The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
  • GO:0009113 The chemical reactions and pathways resulting in the formation of purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records
Show feature table
Start End DB Term Name
2 464 NCBIfam TIGR01134 amidophosphoribosyltransferase
2 464 InterPro IPR005854 Amidophosphoribosyltransferase
273 392 Pfam PF00156 Phosphoribosyl transferase domain
273 392 InterPro IPR000836 Phosphoribosyltransferase domain
250 483 SUPERFAMILY SSF53271 PRTase-like
250 483 InterPro IPR029057 Phosphoribosyltransferase-like
2 266 CDD cd00715 GPATase_N
2 266 InterPro IPR035584 Amidophosphoribosyltransferase, N-terminal
470 490 Coils Coil Coil
2 464 Gene3D G3DSA:3.60.20.10 Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
2 464 InterPro IPR029055 Nucleophile aminohydrolases, N-terminal
1 481 PANTHER PTHR11907 AMIDOPHOSPHORIBOSYLTRANSFERASE
65 200 Pfam PF13522 Glutamine amidotransferase domain
2 257 SUPERFAMILY SSF56235 N-terminal nucleophile aminohydrolases (Ntn hydrolases)
2 257 InterPro IPR029055 Nucleophile aminohydrolases, N-terminal
277 397 CDD cd06223 PRTases_typeI
277 397 InterPro IPR000836 Phosphoribosyltransferase domain
1 481 PIRSF PIRSF000485 Pur1
1 481 InterPro IPR005854 Amidophosphoribosyltransferase
275 444 Gene3D G3DSA:3.40.50.2020 -
275 444 InterPro IPR029057 Phosphoribosyltransferase-like
2 234 ProSiteProfiles PS51278 Glutamine amidotransferase type 2 domain profile.
2 234 InterPro IPR017932 Glutamine amidotransferase type 2 domain
1 464 Hamap MF_01931 Amidophosphoribosyltransferase [purF].
1 464 InterPro IPR005854 Amidophosphoribosyltransferase

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

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA3108
AlphaFold — — full sequence — Viewing
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 0.671

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.

62 records
Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 62 via homologs
Structural ligands 10 0 loaded crystals
Bioactive compounds 2 50 ZINC candidates
Drug-like & clean 14 0 PAINS alerts
Best available ligand signal
5GP PDB via homolog 363.2 Da · LogP -2.57 · TPSA 206.0
5GP PDB via homolog AGP PDB via homolog F6R PDB via homolog G4P PDB via homolog

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
5GP
1ECB
P0AG16 363.2 Da LogP -2.57 TPSA 206.0 1 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…
AGP
1MOS
P17169 261.2 Da LogP -3.50 TPSA 173.7 1 viol. ✓ Clean C([C@@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)…
F6R
4AMV
P17169 260.1 Da LogP -3.26 TPSA 164.8 1 viol. ✓ Clean C([C@H]([C@H]([C@@H](C(=O)CO)O)O)O)OP(=O)(O)O
G4P
6CZF
P0AG16 603.2 Da LogP -2.22 TPSA 345.6 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…
G6Q
1JXA
P17169 260.1 Da LogP -3.26 TPSA 164.8 1 viol. ✓ Clean C([C@H]([C@H]([C@@H]([C@H](C=O)O)O)O)O)OP(=O)(O…
HGA
1XFG
P17169 162.1 Da LogP -1.32 TPSA 112.7 ✓ Ro5 ✓ Clean C(CC(=O)NO)[C@@H](C(=O)O)N
N7Y
6OTT
P0AG16 587.2 Da LogP -1.51 TPSA 325.7 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
ONL
1ECC
P0AG16 145.2 Da LogP -0.23 TPSA 80.4 ✓ Ro5 ✓ Clean CC(=O)CC[C@@H](C(=O)O)N
PCP
1ECC
P0AG16 388.1 Da LogP -1.57 TPSA 220.5 1 viol. ✓ Clean C1[C@@H]([C@H]([C@H]([C@H]1O[P@](=O)(O)OP(=O)(O…
PIN
1ECF
P0AG16 302.4 Da LogP -1.62 TPSA 115.2 ✓ Ro5 ✓ Clean C1CN(CCN1CCS(=O)(=O)O)CCS(=O)(=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.