Protein profile

PA3439

D-erythro-7,8-dihydroneopterin triphosphate 2'-epimerase

Genome: NC_002516.2

Gene: PA3439 folX Structure source: Experimental + AlphaFold UniProt Q9HYG7

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Amino acids 123

Annotations 7

Features 13

PDB binders 2

Druggability 0.688

Overview

Basic information about this protein and its source genome.

Accession: PA3439
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3439 folX
Status: annotated
Amino acids: 123
Structure source: Experimental + AlphaFold

5.1.99.7

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004150 Catalysis of the reaction: 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde. GO:0008719 Catalysis of the reaction: 7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate. GO:0006760 The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units. GO:0006729 The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.

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 0.688

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MPRLEPGMARIRVKDLRLRTFIGIKEEEILNKQDVLINLTILYPAADAVEVNDIEHALNYRTITKAIIRHVEENRFALLERMTQEILDLVMENPAVRYAEVEVDKPHALRFAESVSITLAGHR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

5.1.99.7

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0004150 Catalysis of the reaction: 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.
GO:0008719 Catalysis of the reaction: 7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate.
GO:0006760 The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
GO:0006729 The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.

Sequence Features

Domain/signature hits from InterPro and related databases.

13 records

Show feature table

Start	End	DB	Term	Name
6	122	Gene3D	G3DSA:3.30.1130.10	-
6	122	InterPro	IPR043133	GTP cyclohydrolase I, C-terminal/NADPH-dependent 7-cyano-7-deazaguanine reductase
4	123	FunFam	G3DSA:3.30.1130.10:FF:000005	D-erythro-7,8-dihydroneopterin triphosphate epimerase
7	120	SUPERFAMILY	SSF55620	Tetrahydrobiopterin biosynthesis enzymes-like
11	121	SMART	SM00905	FolB_2
11	121	InterPro	IPR006157	Dihydroneopterin aldolase/epimerase domain
6	120	PANTHER	PTHR42844	DIHYDRONEOPTERIN ALDOLASE 1-RELATED
6	120	InterPro	IPR006156	Dihydroneopterin aldolase
8	119	NCBIfam	TIGR00526	FolB domain
8	119	InterPro	IPR006157	Dihydroneopterin aldolase/epimerase domain
8	119	CDD	cd00534	DHNA_DHNTPE
11	119	Pfam	PF02152	Dihydroneopterin aldolase
11	119	InterPro	IPR006157	Dihydroneopterin aldolase/epimerase domain

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

1 + 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 4AEY	X-ray	3.00 Å	A	100.0% 1-123	PDBe RCSB PDBj File	Viewing
AlphaFold PA3439	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				0.688
2				0.229

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				2.14	0.05

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				0.377

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.

27 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.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
NEU	2O90	P0AC16	253.2 Da LogP -2.32 TPSA 158.2	✓ Ro5	✓ Clean	`c1c(nc2c(n1)N=C(NC2=O)N)[C@@H]([C@@H](CO)O)O`
PE0	6OJO	A0A5P8YJX5	163.1 Da LogP -0.70 TPSA 97.5	✓ Ro5	✓ Clean	`c1cnc2c(n1)C(=O)NC(=N2)N`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC12428336	1.000	253.2 Da LogP -2.32 TPSA 158.2	✓ Ro5	✓ Clean	`Nc1nc2ncc([C@H](O)[C@H](O)CO)nc2c(=O)[nH]1`
ZINC17176122	1.000	253.2 Da LogP -2.32 TPSA 158.2	✓ Ro5	✓ Clean	`Nc1nc2ncc([C@@H](O)[C@@H](O)CO)nc2c(=O)[nH]1`
ZINC17176123	1.000	253.2 Da LogP -2.32 TPSA 158.2	✓ Ro5	✓ Clean	`Nc1nc2ncc([C@H](O)[C@@H](O)CO)nc2c(=O)[nH]1`
ZINC18169010	1.000	253.2 Da LogP -2.32 TPSA 158.2	✓ Ro5	✓ Clean	`Nc1nc2ncc([C@@H](O)[C@H](O)CO)nc2c(=O)[nH]1`
ZINC17129255	0.738	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H](O)c1cnc2nc(N)[nH]c(=O)c2n1`
ZINC17129257	0.738	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H](O)c1cnc2nc(N)[nH]c(=O)c2n1`
ZINC17129259	0.738	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](O)c1cnc2nc(N)[nH]c(=O)c2n1`
ZINC18275062	0.738	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@H](O)[C@H](O)c1cnc2nc(N)[nH]c(=O)c2n1`
ZINC7998083	0.705	267.2 Da LogP -1.93 TPSA 158.2	✓ Ro5	✓ Clean	`C[C@H](O)[C@H](O)[C@@H](O)c1cnc2nc(N)[nH]c(=O)c…`
ZINC8568890	0.705	267.2 Da LogP -1.93 TPSA 158.2	✓ Ro5	✓ Clean	`C[C@H](O)[C@H](O)[C@H](O)c1cnc2nc(N)[nH]c(=O)c2…`
ZINC8602624	0.705	267.2 Da LogP -1.93 TPSA 158.2	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H](O)[C@H](O)c1cnc2nc(N)[nH]c(=O)c…`
ZINC5807319	0.674	284.3 Da LogP -1.18 TPSA 132.2	✓ Ro5	✓ Clean	`CSc1nc2ncc([C@H](O)[C@H](O)CO)nc2c(=O)[nH]1`
ZINC5807320	0.674	284.3 Da LogP -1.18 TPSA 132.2	✓ Ro5	✓ Clean	`CSc1nc2ncc([C@H](O)[C@@H](O)CO)nc2c(=O)[nH]1`
ZINC5807321	0.674	284.3 Da LogP -1.18 TPSA 132.2	✓ Ro5	✓ Clean	`CSc1nc2ncc([C@@H](O)[C@H](O)CO)nc2c(=O)[nH]1`
ZINC5807322	0.674	284.3 Da LogP -1.18 TPSA 132.2	✓ Ro5	✓ Clean	`CSc1nc2ncc([C@@H](O)[C@@H](O)CO)nc2c(=O)[nH]1`
ZINC17429362	0.591	207.2 Da LogP -1.17 TPSA 117.8	✓ Ro5	✓ Clean	`Nc1nc2ncc(CCO)nc2c(=O)[nH]1`
ZINC14420733	0.587	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H](O)c1cnc2c(=O)[nH]c(N)nc2n1`
ZINC17860887	0.587	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@H](O)[C@H](O)c1cnc2c(=O)[nH]c(N)nc2n1`
ZINC17994680	0.587	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H](O)c1cnc2c(=O)[nH]c(N)nc2n1`
ZINC18036401	0.587	237.2 Da LogP -1.29 TPSA 138.0	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H](O)c1cnc2c(=O)[nH]c(N)nc2n1`
ZINC5127809	0.541	207.1 Da LogP -1.01 TPSA 134.8	✓ Ro5	✓ Clean	`Nc1nc2ncc(C(=O)O)nc2c(=O)[nH]1`
ZINC142664839	0.533	211.6 Da LogP 0.03 TPSA 97.5	✓ Ro5	✓ Clean	`Nc1nc2ncc(CCl)nc2c(=O)[nH]1`
ZINC26466141	0.528	224.2 Da LogP 1.38 TPSA 71.5	✓ Ro5	✓ Clean	`O=c1[nH]c(-c2ccccc2)nc2nccnc12`
ZINC17013463	0.514	208.2 Da LogP 0.83 TPSA 71.5	✓ Ro5	✓ Clean	`CCSc1nc2nccnc2c(=O)[nH]1`
ZINC142782797	0.500	303.1 Da LogP 2.14 TPSA 71.5	✓ Ro5	✓ Clean	`O=c1[nH]c(-c2ccc(Br)cc2)nc2nccnc12`

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.