Protein profile

PA4415

phospho-N-acetylmuramoyl-pentapeptide- transferase

Genome: NC_002516.2

Gene: PA4415 mraY Structure source: AlphaFold UniProt Q9HVZ8

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Amino acids 360

Annotations 12

Features 45

PDB binders 2

Druggability 0.914

Overview

Basic information about this protein and its source genome.

Accession: PA4415
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4415 mraY
Status: annotated
Amino acids: 360
Structure source: AlphaFold

2.7.8.13

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0046872 Binding to a metal ion. GO:0008963 Catalysis of the reaction: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine = Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + UMP. GO:0051992 Catalysis of the reaction: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP. 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:0044038 The chemical reactions and pathways resulting in the formation of a macromolecule destined to form part of a cell wall.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: CytoplasmicMembrane

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 0.914

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Enzyme Commission (EC)

2.7.8.13

Gene Ontology (GO)

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0046872 Binding to a metal ion.
GO:0008963 Catalysis of the reaction: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine = Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + UMP.
GO:0051992 Catalysis of the reaction: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP.
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:0044038 The chemical reactions and pathways resulting in the formation of a macromolecule destined to form part of a cell wall.
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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0016780 Catalysis of the transfer of a substituted phosphate group, other than diphosphate or nucleotidyl residues, from one compound (donor) to a another (acceptor).

Sequence Features

Domain/signature hits from InterPro and related databases.

45 records

Show feature table

Start	End	DB	Term	Name
289	311	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
194	199	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
285	289	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
189	200	ProSitePatterns	PS01348	MraY family signature 2.
189	200	InterPro	IPR018480	Phospho-N-acetylmuramoyl-pentapeptide transferase, conserved site
42	72	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
97	114	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
61	356	CDD	cd06852	GT_MraY
61	356	InterPro	IPR003524	Phospho-N-acetylmuramoyl-pentapeptide transferase
338	357	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
115	133	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
358	360	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
71	90	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
92	96	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
220	238	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
200	222	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
200	219	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
263	284	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
168	185	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
73	91	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
312	337	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
172	193	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
290	311	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
239	256	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
134	156	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
338	357	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
99	284	Pfam	PF00953	Glycosyl transferase family 4
99	284	InterPro	IPR000715	Glycosyl transferase, family 4
37	360	NCBIfam	TIGR00445	phospho-N-acetylmuramoyl-pentapeptide-transferase
37	360	InterPro	IPR003524	Phospho-N-acetylmuramoyl-pentapeptide transferase
20	41	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
21	43	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	19	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
257	262	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
68	80	ProSitePatterns	PS01347	MraY family signature 1.
68	80	InterPro	IPR018480	Phospho-N-acetylmuramoyl-pentapeptide transferase, conserved site
262	284	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
97	114	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
25	358	Hamap	MF_00038	Phospho-N-acetylmuramoyl-pentapeptide-transferase [mraY].
25	358	InterPro	IPR003524	Phospho-N-acetylmuramoyl-pentapeptide transferase
25	357	PANTHER	PTHR22926	PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
25	357	InterPro	IPR000715	Glycosyl transferase, family 4
134	152	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
235	257	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
153	171	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

3D Structure

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

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Structural evidence

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA4415	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				0.914
3				0.869
6				0.582
9				0.205

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.

36 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
NK4	6OYH	O66465	798.0 Da LogP 1.05 TPSA 250.3	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCC[C@H]1CN([C@H](C(=O)N([C@@H]1C…`
NKD	6OZ6	O66465	856.9 Da LogP -1.83 TPSA 328.0	3 viol.	✓ Clean	`C[C@@H]([C@@H](C(=O)N/C=C\1/[C@H]([C@H]([C@@H](…`

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
CHEMBL4286766	P0C1R8	10.80	946.0 Da LogP -6.69 TPSA 432.6	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL4279378	P0C1R8	10.66	1156.3 Da LogP -1.58 TPSA 438.7	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL4284923	P0C1R8	10.03	988.0 Da LogP -6.51 TPSA 435.7	3 viol.	✓ Clean	`CO[C@H]1[C@H](O[C@H]([C@H]2O[C@@H](n3ccc(=O)[nH…`
CHEMBL4475677	P0C1R8	8.59	784.0 Da LogP 0.71 TPSA 259.1	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCC[C@@H]1CN[C@@H]([C@H](O[C@@H]2…`
57M	Q03521	8.12	916.0 Da LogP -6.52 TPSA 425.9	3 viol.	✓ Clean	`CC(C)C[C@@H](C(=O)NCCCN[C@@H]([C@@H]([C@@H]1[C@…`
CHEMBL5282738	E2QF15	8.00	649.7 Da LogP -3.07 TPSA 242.8	3 viol.	✓ Clean	`CO[C@H]1[C@@H](OC)[C@H](n2ccc(=O)[nH]c2=O)O[C@@…`
CHEMBL5265940	P0C1R8	7.77	583.6 Da LogP -4.18 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@@H](O)[C@H](n2ccc(=O)[nH]c2=O)O[C@@H…`
CHEMBL95027	P0A6W3	7.77	583.6 Da LogP -4.18 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@@H](O)[C@H](n2ccc(=O)[nH]c2=O)O[C@@H…`
CHEMBL2048825	P0C1R8	7.66	711.7 Da LogP -1.68 TPSA 283.1	3 viol.	✓ Clean	`C[C@H](N)C(=O)N(C)[C@@H](C)[C@H](NC(=O)[C@H](C)…`
CHEMBL2048828	P0C1R8	7.66	876.9 Da LogP -2.67 TPSA 352.6	3 viol.	✓ Clean	`C[C@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)C…`
CHEMBL5272467	Q03521	7.66	726.7 Da LogP -2.74 TPSA 309.1	3 viol.	✓ Clean	`C[C@@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)…`
CHEMBL4473600	P0C1R8	7.62	711.9 Da LogP 0.66 TPSA 230.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)N[C@H]1CCN[C@H]([C@H](O[C@@…`
CHEMBL5277590	P0C1R8	7.57	473.4 Da LogP -4.18 TPSA 221.9	1 viol.	✓ Clean	`COC(=O)C1=C[C@@H](O)[C@@H](O)[C@H](O[C@@H](C(N)…`
CHEMBL2048826	P0C1R8	7.38	727.7 Da LogP -2.71 TPSA 303.3	3 viol.	✓ Clean	`C[C@H](N)C(=O)N(C)[C@@H](C)[C@H](NC(=O)[C@H](C)…`
CHEMBL5271984	Q03521	7.38	713.7 Da LogP -3.05 TPSA 312.1	3 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@@H](C)[C@H](NC(=O)[C@H](C)NC(…`
CHEMBL1780217	Q03521	7.31	916.0 Da LogP -6.31 TPSA 423.4	3 viol.	✓ Clean	`CC(C)C[C@@H](NC(=O)[C@@H](NC(=O)N[C@H](C(=O)O)C…`
CHEMBL5278937	E2QF15	7.24	601.6 Da LogP -4.62 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@@H](O)[C@H](n2ccc(=O)[nH]c2=O)O[C@@H…`
CHEMBL2048830	P0C1R8	7.19	713.7 Da LogP -3.10 TPSA 303.3	3 viol.	✓ Clean	`C[C@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)C…`
CHEMBL1780218	Q03521	6.61	1070.3 Da LogP -1.88 TPSA 423.4	3 viol.	✓ Clean	`CCCCCCCCCCCCCCC[C@H](NC(=O)[C@@H](NC(=O)N[C@H](…`
9LH	P0C1R8	6.60	830.9 Da LogP -2.48 TPSA 311.8	3 viol.	✓ Clean	`CC(C)CCCCCCCCC/C=C/C(=O)N[C@@H]1[C@H]([C@H]([C@…`
CHEMBL5279603	P0C1R8	6.52	490.5 Da LogP -3.42 TPSA 215.5	2 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(N)cc2)[C@H]2O[…`
CHEMBL5267618	P0A6W3	6.48	502.6 Da LogP -2.49 TPSA 201.5	3 viol.	✓ Clean	`CCCCCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@H]1O)[…`
CHEMBL5275061	P0A6W3	6.48	586.7 Da LogP -0.15 TPSA 201.5	3 viol.	✓ Clean	`CCCCCCCCCCCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@…`
CHEMBL5276993	P0A6W3	6.48	558.7 Da LogP -0.93 TPSA 201.5	3 viol.	✓ Clean	`CCCCCCCCCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@H]…`
CHEMBL5281271	P0A6W3	6.48	460.5 Da LogP -3.66 TPSA 201.5	2 viol.	✓ Clean	`CCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@H]1O)[C@H…`
CHEMBL5288850	P0A6W3	6.48	530.6 Da LogP -1.71 TPSA 201.5	3 viol.	✓ Clean	`CCCCCCCCCNCC(O[C@@H]1O[C@H](CN)[C@@H](O)[C@H]1O…`
NKM	P0C1R8	6.48	569.5 Da LogP -4.57 TPSA 253.8	3 viol.	✓ Clean	`CO[C@H]1[C@H]([C@@H](O[C@@H]1[C@H](C(=O)N)O[C@@…`
CHEMBL5289885	P0C1R8	6.23	551.6 Da LogP -1.33 TPSA 189.5	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(-c3ccccc3)cc2)…`
CHEMBL2048831	P0C1R8	6.19	876.9 Da LogP -2.67 TPSA 352.6	3 viol.	✓ Clean	`C[C@H](NC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O)C…`
CHEMBL5277496	P0C1R8	6.19	551.6 Da LogP -1.33 TPSA 189.5	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2cccc(-c3ccccc3)c2)…`
CHEMBL1780219	Q03521	6.16	1070.3 Da LogP -1.88 TPSA 423.4	3 viol.	✓ Clean	`CCCCCCCCCCCCCCC[C@@H](NC(=O)[C@@H](NC(=O)N[C@H]…`
CHEMBL5287014	P0C1R8	6.05	594.6 Da LogP -1.75 TPSA 218.6	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(C(=O)Nc3ccccc3…`
CHEMBL5268197	P0C1R8	6.02	630.6 Da LogP -2.20 TPSA 235.7	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2cccc(NS(=O)(=O)c3c…`
CHEMBL5291217	P0C1R8	6.00	630.6 Da LogP -2.20 TPSA 235.7	3 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H](C#Cc2ccc(NS(=O)(=O)c3cc…`

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

No virtual-screening candidates for this protein.

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.