Protein profile

PA4411

UDP-N-acetylmuramate--L-alanine ligase

Genome: NC_002516.2

Gene: murC PA4411 Structure source: Experimental + AlphaFold UniProt Q9HW02
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Amino acids 480
Annotations 10
Features 26
PDB binders 7
Druggability 0.918

Overview

Basic information about this protein and its source genome.

Accession
PA4411
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
murC PA4411
Status
annotated
Amino acids
480
Structure source
Experimental + AlphaFold
EC
6.3.2.8
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0008763 Catalysis of the reaction: L-alanine + ATP + UDP-N-acetylmuramate = ADP + 2 H+ + phosphate + UDP-N-acetylmuramoyl-L-alanine. 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.

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 0.918
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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0008763 Catalysis of the reaction: L-alanine + ATP + UDP-N-acetylmuramate = ADP + 2 H+ + phosphate + UDP-N-acetylmuramoyl-L-alanine.
  • 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:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
  • GO:0016881 Catalysis of the ligation of an acid to an amino acid via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records
Show feature table
Start End DB Term Name
104 320 FunFam G3DSA:3.40.1190.10:FF:000001 UDP-N-acetylmuramate--L-alanine ligase
322 473 Gene3D G3DSA:3.90.190.20 -
322 473 InterPro IPR036615 Mur ligase, C-terminal domain superfamily
1 19 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
15 472 Hamap MF_00046 UDP-N-acetylmuramate--L-alanine ligase [murC].
15 472 InterPro IPR005758 UDP-N-acetylmuramate--L-alanine ligase
20 40 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
16 102 SUPERFAMILY SSF51984 MurCD N-terminal domain
41 480 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
7 102 Gene3D G3DSA:3.40.50.720 -
12 468 PANTHER PTHR43445 UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED
101 318 SUPERFAMILY SSF53623 MurD-like peptide ligases, catalytic domain
101 318 InterPro IPR036565 Mur-like, catalytic domain superfamily
120 299 Pfam PF08245 Mur ligase middle domain
120 299 InterPro IPR013221 Mur ligase, central
319 468 SUPERFAMILY SSF53244 MurD-like peptide ligases, peptide-binding domain
319 468 InterPro IPR036615 Mur ligase, C-terminal domain superfamily
17 115 Pfam PF01225 Mur ligase family, catalytic domain
17 115 InterPro IPR000713 Mur ligase, N-terminal catalytic domain
104 321 Gene3D G3DSA:3.40.1190.10 -
104 321 InterPro IPR036565 Mur-like, catalytic domain superfamily
320 410 Pfam PF02875 Mur ligase family, glutamate ligase domain
320 410 InterPro IPR004101 Mur ligase, C-terminal
20 42 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
17 466 NCBIfam TIGR01082 UDP-N-acetylmuramate--L-alanine ligase
17 466 InterPro IPR005758 UDP-N-acetylmuramate--L-alanine ligase

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

9 + 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 8DOF
X-ray 2.60 Å A
100.0% 1-480
PDBe RCSB PDBj File
Viewing
PDB 6X9N
X-ray 2.25 Å A,B,C,D,E,F,G,H
96.9% 16-480
PDBe RCSB PDBj File
Loaded
PDB 6X9F
X-ray 2.35 Å A,B,C,D,E,F,G,H
96.9% 16-480
PDBe RCSB PDBj File
Loaded
PDB 8EWA
X-ray 1.85 Å A,B
64.0% 16-322
PDBe RCSB PDBj File
Loaded
PDB 8EGN
X-ray 1.95 Å A,B
64.0% 16-322
PDBe RCSB PDBj File
Loaded
PDB 8EGM
X-ray 2.20 Å A,B,C,D,E,F,G,H
64.0% 16-322
PDBe RCSB PDBj File
Loaded
PDB 5VVW
X-ray 2.30 Å A,B,C,D,E,F,G,H
64.0% 16-322
PDBe RCSB PDBj File
Loaded
PDB 9D9M
X-ray 2.32 Å A
64.0% 16-322
PDBe RCSB PDBj File
Loaded
PDB 9D9K
X-ray 2.63 Å A
64.0% 16-322
PDBe RCSB PDBj File
Metadata only
AlphaFold PA4411
AlphaFold — — full sequence — Loaded
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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.

57 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
UXP
6X9F 2.35 Å Open crystal
354.4 Da LogP 2.05 TPSA 118.6 ✓ Ro5 ✓ Clean c1c([nH]nc1Nc2c3c[nH]nc3nc(n2)N4CCCC[C@@H]4CO)C…
UYD
6X9N 2.25 Å Open crystal
406.5 Da LogP 3.27 TPSA 116.6 ✓ Ro5 ✓ Clean CC(C)(C)c1cc(nn1C)Nc2c3cn[nH]c3nc(n2)N[C@@H](CO…

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.