Protein profile

PA4450

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Genome: NC_002516.2

Gene: murA PA4450 Structure source: Experimental + AlphaFold UniProt Q9HVW7

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Amino acids 421

Annotations 10

Features 16

PDB binders 17

Druggability 0.734

Overview

Basic information about this protein and its source genome.

Accession: PA4450
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: murA PA4450
Status: annotated
Amino acids: 421
Structure source: Experimental + AlphaFold

2.5.1.7

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0008760 Catalysis of the reaction: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine. GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides. GO:0008360 Any process that modulates the surface configuration of a cell.

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 0.734

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MDKLIITGGNRLDGEIRISGAKNSALPILAATLLADTPVTVCNLPHLHDITTMIELFGRMGVQPIIDEKLNVEVDASSIKTLVAPYELVKTMRASILVLGPMLARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAQIEVEGGYIKAKAPAGGLRGGHFFFDTVSVTGTENLMMAAALANGRTVLQNAAREPEVVDLANCLNAMGANVQGAGSDTIVIEGVKRLGGARYDVLPDRIETGTYLVAAAATGGRVKLKDTDPTILEAVLQKLEEAGAHISTGSNWIELDMKGNRPKAVNVRTAPYPAFPTDMQAQFISMNAVAEGTGAVIETVFENRFMHVYEMNRMGAQILVEGNTAIVTGVPKLKGAPVMATDLRASASLVIAGLVAEGDTLIDRIYHIDRGYECIEEKLQLLGAKIRRVPG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

2.5.1.7

Gene Ontology (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:0008760 Catalysis of the reaction: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine.
GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
GO:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
GO:0008360 Any process that modulates the surface configuration of a cell.
GO:0019277 The chemical reactions and pathways resulting in the formation of UDP-N-acetylgalactosamine, a substance composed of N-acetylgalactosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
GO:0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
21	231	Gene3D	G3DSA:3.65.10.10	Enolpyruvate transferase domain
21	231	InterPro	IPR036968	Enolpyruvate transferase domain superfamily
12	412	CDD	cd01555	UdpNAET
12	412	InterPro	IPR005750	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
1	419	Hamap	MF_00111	UDP-N-acetylglucosamine 1-carboxyvinyltransferase [murA].
1	419	InterPro	IPR005750	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
4	416	Gene3D	G3DSA:3.65.10.10	Enolpyruvate transferase domain
4	416	InterPro	IPR036968	Enolpyruvate transferase domain superfamily
7	409	Pfam	PF00275	EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
7	409	InterPro	IPR001986	Enolpyruvate transferase domain
2	420	PANTHER	PTHR43783	UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE
217	417	FunFam	G3DSA:3.65.10.10:FF:000002	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
1	418	NCBIfam	TIGR01072	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
1	418	InterPro	IPR005750	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
1	419	SUPERFAMILY	SSF55205	EPT/RTPC-like
1	419	InterPro	IPR013792	RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta

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 5BQ2	X-ray	1.70 Å	A,B,C,D	100.0% 1-421	PDBe RCSB PDBj File	Viewing
AlphaFold PA4450	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				0.734
3				0.318

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	Score	Probability
1	42.72	0.968
2	5.27	0.247
3	3.11	0.104
4	1.41	0.018

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				0.783
9				0.327

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.

73 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.

Ligand	Source crystal	MW · LogP · TPSA	Lipinski	PAINS	SMILES
EPU	5BQ2 1.70 Å Open crystal	677.4 Da LogP -4.03 TPSA 332.2	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`

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
0V5	6CN1	Q88P88	170.1 Da LogP -0.43 TPSA 104.1	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)OP(=O)(O)O`
2AN	1EYN	P33038	299.4 Da LogP 3.83 TPSA 66.4	✓ Ro5	✓ Clean	`c1ccc(cc1)Nc2cccc3c2c(ccc3)S(=O)(=O)O`
EPZ	3SU9	P33038	679.4 Da LogP -4.15 TPSA 332.2	3 viol.	✓ Clean	`C[C@H](C(=O)O)O[C@@H]1[C@H]([C@H](O[C@@H]([C@H]…`
FFQ	3LTH	P33038	140.1 Da LogP -0.11 TPSA 77.8	✓ Ro5	✓ Clean	`CC[C@H](O)P(=O)(O)O`
HAI	1DLG	P33038	100.2 Da LogP 0.56 TPSA 27.6	✓ Ro5	✓ Clean	`C1CCC(CC1)[NH3+]`
MOE	3SWI	P33038	75.1 Da LogP -1.01 TPSA 32.3	✓ Ro5	✓ Clean	`COCC[O-]`
PG0	3SWI	P33038	120.1 Da LogP -0.36 TPSA 38.7	✓ Ro5	✓ Clean	`COCCOCCO`
PO3	3ISS	P0A749	79.0 Da LogP -1.64 TPSA 63.2	✓ Ro5	✓ Clean	`[O-][P-](=O)[O-]`
TAV	1YBG	P33038	662.7 Da LogP 4.56 TPSA 184.4	1 viol.	✓ Clean	`CN([C@@H](CC(=O)O)C(=O)O)C(=O)c1cc(ccc1NS(=O)(=…`
TET	1A2N	P0A749	793.4 Da LogP -4.77 TPSA 398.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`
TR9	3KQA	P33038	156.1 Da LogP -0.28 TPSA 74.6	✓ Ro5	✓ Clean	`CC1=C(C(=O)C[C@@H](C1=O)O)O`
UD1	3LTH	P33038	607.4 Da LogP -4.65 TPSA 305.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`
UD2	3SWI	P33038	607.4 Da LogP -4.65 TPSA 305.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@H]([C@H](O[C@@H]1O[P@@](…`
UDA	1Q3G	P33038	775.4 Da LogP -4.72 TPSA 398.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`
UPG	4E7B	P33038	566.3 Da LogP -4.79 TPSA 297.0	3 viol.	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
UPN	3SWI	P33038	677.4 Da LogP -4.03 TPSA 332.2	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@H]([C@H](O[C@@H]1O[P@](=…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
FCN	P0A749	7.00	138.1 Da LogP -0.09 TPSA 70.1	✓ Ro5	✓ Clean	`C[C@H]1[C@H](O1)P(=O)(O)O`
CHEMBL1200331	P0A749	—	259.2 Da LogP -2.43 TPSA 156.8	1 viol.	✓ Clean	`C[C@@H]1O[C@@H]1P(=O)(O)O.NC(CO)(CO)CO`
CHEMBL2335230	P0A749	—	296.9 Da LogP 3.01 TPSA 56.3	✓ Ro5	✓ Clean	`O=[N+]([O-])/C(Br)=C/c1ccc(Br)o1`
CHEMBL5219390	P0A749	—	509.0 Da LogP 6.45 TPSA 92.9	2 viol.	✓ Clean	`CC(C)(C)OC(=O)C1=C(O)C(=O)N(c2nc3ccccc3s2)C1c1c…`
CHEMBL5417308	P0A749	—	229.8 Da LogP 2.70 TPSA 29.1	✓ Ro5	✓ Clean	`O=C(CCl)NC1CCCC2CCCCC21`
FOM	P0A749	—	183.1 Da LogP -0.60 TPSA 98.1	✓ Ro5	✓ Clean	`C(CN(C=O)O)CP(=O)(O)O`

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
ZINC1532216	1.000	299.4 Da LogP 3.83 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)c1cccc2cccc(Nc3ccccc3)c12`
ZINC1580161	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC7571	1.000	296.9 Da LogP 3.01 TPSA 56.3	✓ Ro5	✓ Clean	`O=[N+]([O-])/C(Br)=C/c1ccc(Br)o1`
ZINC1712810	0.757	313.4 Da LogP 4.14 TPSA 66.4	✓ Ro5	✓ Clean	`Cc1ccc(Nc2cccc3cccc(S(=O)(=O)O)c23)cc1`
ZINC575419714	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC115163232	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC258837490	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC5162495	0.697	249.3 Da LogP 2.68 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)c1ccccc1Nc1ccccc1`
ZINC12501520	0.688	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1692489	0.688	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC3874716	0.688	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769	0.688	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548	0.688	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC4530388	0.688	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5178829	0.688	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830	0.688	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5701172	0.688	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861	0.688	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC2053549711	0.676	232.0 Da LogP 2.68 TPSA 56.3	✓ Ro5	✓ Clean	`CC(=Cc1ccc(Br)o1)[N+](=O)[O-]`
ZINC34984414	0.676	232.0 Da LogP 2.68 TPSA 56.3	✓ Ro5	✓ Clean	`C/C(=C\c1ccc(Br)o1)[N+](=O)[O-]`
ZINC575432150	0.667	344.4 Da LogP -0.89 TPSA 100.5	✓ Ro5	✓ Clean	`COCCOCCOCCS(=O)(=O)CCOCCOCCO`
ZINC1857524240	0.652	207.3 Da LogP -0.75 TPSA 60.0	✓ Ro5	✓ Clean	`COCCNCCOCCOCCO`
ZINC71772395	0.605	265.3 Da LogP 2.04 TPSA 83.5	✓ Ro5	✓ Clean	`CC(=O)Nc1cccc2cccc(S(=O)(=O)O)c12`
ZINC5650743	0.600	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917	0.600	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC116981890	0.594	288.3 Da LogP 1.33 TPSA 108.7	✓ Ro5	✓ Clean	`O=S(=O)(O)c1cccc2cccc(S(=O)(=O)O)c12`
ZINC116078641	0.583	222.2 Da LogP -0.80 TPSA 74.2	✓ Ro5	✓ Clean	`COC(=O)COCCOCCOCCO`
ZINC1857790631	0.583	280.3 Da LogP -0.39 TPSA 83.5	✓ Ro5	✓ Clean	`COC(=O)CCOCCOCCOCCOCCO`
ZINC196151418	0.583	266.3 Da LogP -0.78 TPSA 83.5	✓ Ro5	✓ Clean	`COC(=O)COCCOCCOCCOCCO`
ZINC202958272	0.583	236.3 Da LogP -0.41 TPSA 74.2	✓ Ro5	✓ Clean	`COC(=O)CCOCCOCCOCCO`
ZINC34111591	0.583	207.3 Da LogP -1.06 TPSA 62.2	✓ Ro5	✓ Clean	`COCCOCCN(CCO)CCO`
ZINC642881862	0.583	324.4 Da LogP -0.38 TPSA 92.7	✓ Ro5	✓ Clean	`COC(=O)CCOCCOCCOCCOCCOCCO`
ZINC2169453	0.575	266.3 Da LogP 1.46 TPSA 92.4	✓ Ro5	✓ Clean	`NCCNc1cccc2cccc(S(=O)(=O)O)c12`
ZINC5575424	0.565	200.0 Da LogP -1.37 TPSA 141.4	✓ Ro5	✓ Clean	`O=C(O)C(OP(=O)(O)O)C(=O)O`
ZINC22590709	0.561	312.4 Da LogP 3.54 TPSA 72.2	✓ Ro5	✓ Clean	`Cc1ccc(Nc2cccc3cccc(S(N)(=O)=O)c23)cc1`
ZINC1586638	0.559	223.4 Da LogP 3.26 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H]1CCCC[C@H]1C1CCCCC1`
ZINC1586639	0.559	223.4 Da LogP 3.26 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1CCCC[C@H]1C1CCCCC1`
ZINC1586640	0.559	223.4 Da LogP 3.26 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H]1CCCC[C@@H]1C1CCCCC1`
ZINC1586641	0.559	223.4 Da LogP 3.26 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H]1CCCC[C@@H]1C1CCCCC1`
ZINC139635624	0.556	207.3 Da LogP 2.65 TPSA 29.1	✓ Ro5	✓ Clean	`C=CC(=O)N[C@@H]1CCC[C@H]2CCCC[C@@H]21`
ZINC139635897	0.556	207.3 Da LogP 2.65 TPSA 29.1	✓ Ro5	✓ Clean	`C=CC(=O)N[C@@H]1CCC[C@@H]2CCCC[C@@H]21`
ZINC141055552	0.556	207.3 Da LogP 2.65 TPSA 29.1	✓ Ro5	✓ Clean	`C=CC(=O)N[C@@H]1CCC[C@@H]2CCCC[C@H]21`
ZINC141055927	0.556	207.3 Da LogP 2.65 TPSA 29.1	✓ Ro5	✓ Clean	`C=CC(=O)N[C@@H]1CCC[C@H]2CCCC[C@H]21`
ZINC13548378	0.551	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=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.