Protein profile

PA1812

membrane-bound lytic murein transglycosylase D

Genome: NC_002516.2

Gene: mltD PA1812 Structure source: Experimental + AlphaFold UniProt Q9I2T2
Export view
Amino acids 534
Annotations 5
Features 49
PDB binders 1
Druggability 0.703

Overview

Basic information about this protein and its source genome.

Accession
PA1812
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
mltD PA1812
Status
annotated
Amino acids
534
Structure source
Experimental + AlphaFold
GO
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0008932 Catalysis of the endolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue. GO:0046872 Binding to a metal ion. GO:0000270 The chemical reactions and pathways involving peptidoglycans, any of a class of glycoconjugates found only 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:0008933 Catalysis of the cleavage of a peptidoglycan chain into a peptidoglycan chain with N-acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a peptidoglycan chain with N-acetylglucosamine at the non-reducing end. Includes endolytic transglycosylase activity that fragments the glycan chain internally and exolytic transgylcosylase activity that cleaves a terminal disaccharide from the end of the glycan strand.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Unknown

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 0.703
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MPPQTRKTPDLDALARAVRVSILLIAGALAGCQGSGQIKGEAQAKAARPGARAVDVQFNPSWLHTQPGQNAAYNDIWDRMRDGFQLQDAISTNPRIERQRLWFLSNQSFLEQSSARGSLYMHYVVERLEERNMPLELALLPVIESAYNPFALSRSNAAGLWQFIPATGQHFNLRQTNFYDGRRDITASTNAALTYLERLHDMFNGDWMLALAAYNAGEGTVSRAIERNEKLGLPTDYWNLPLPQETQDYVPKLLALSQIVMAPDSYGISLNPINNEPYFQAVRVKRGIDLSSVAALANLDEDELYQLNPAYKRRVTMDGPQQLLVPMEKAAFLTASLDTLKPKEVTAWQQYRVRSGDSLHSIANRYRITVAELKSANRLSSNHLRKGQQLSIPGQIAGGAVKPVYQQLARQASTPARTRSYKVKNGDSLWQIARNNGVDVNDLKRWNGLDKHALKVGQTLKLQGGTQALAARKGNAAGKRDSATYYKVKQGDSMYLIAKRFNVEMKHLQRWNPRSKQALKPGQTLTLYLDTASR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0008932 Catalysis of the endolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
  • GO:0046872 Binding to a metal ion.
  • GO:0000270 The chemical reactions and pathways involving peptidoglycans, any of a class of glycoconjugates found only 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:0008933 Catalysis of the cleavage of a peptidoglycan chain into a peptidoglycan chain with N-acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a peptidoglycan chain with N-acetylglucosamine at the non-reducing end. Includes endolytic transglycosylase activity that fragments the glycan chain internally and exolytic transgylcosylase activity that cleaves a terminal disaccharide from the end of the glycan strand.

Sequence Features

Domain/signature hits from InterPro and related databases.

49 records
Show feature table
Start End DB Term Name
349 393 SUPERFAMILY SSF54106 LysM domain
349 393 InterPro IPR036779 LysM domain superfamily
140 168 ProSitePatterns PS00922 Prokaryotic transglycosylases signature.
140 168 InterPro IPR000189 Prokaryotic transglycosylase, active site
1 30 SignalP_EUK SignalP-noTM SignalP-noTM
120 279 SUPERFAMILY SSF53955 Lysozyme-like
120 279 InterPro IPR023346 Lysozyme-like domain superfamily
484 528 SUPERFAMILY SSF54106 LysM domain
484 528 InterPro IPR036779 LysM domain superfamily
128 258 CDD cd16894 MltD-like
486 526 Pfam PF01476 LysM domain
486 526 InterPro IPR018392 LysM domain
421 462 Pfam PF01476 LysM domain
421 462 InterPro IPR018392 LysM domain
351 393 Pfam PF01476 LysM domain
351 393 InterPro IPR018392 LysM domain
118 265 Gene3D G3DSA:1.10.530.10 -
1 34 Pfam PF06474 MltD lipid attachment motif
1 34 InterPro IPR010511 Lytic murein transglycosylase D , lipid attachment domain
278 394 PANTHER PTHR33734 LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2
116 269 FunFam G3DSA:1.10.530.10:FF:000004 Membrane-bound lytic murein transglycosylase D
348 395 Gene3D G3DSA:3.10.350.10 LysM domain
348 395 InterPro IPR036779 LysM domain superfamily
417 467 Gene3D G3DSA:3.10.350.10 LysM domain
417 467 InterPro IPR036779 LysM domain superfamily
343 395 FunFam G3DSA:3.10.350.10:FF:000014 Soluble lytic murein transglycosylase
349 392 ProSiteProfiles PS51782 LysM domain profile.
349 392 InterPro IPR018392 LysM domain
131 230 Pfam PF01464 Transglycosylase SLT domain
131 230 InterPro IPR008258 Transglycosylase SLT domain 1
484 527 ProSiteProfiles PS51782 LysM domain profile.
484 527 InterPro IPR018392 LysM domain
484 527 CDD cd00118 LysM
420 463 SMART SM00257 LysM_2
420 463 InterPro IPR018392 LysM domain
485 528 SMART SM00257 LysM_2
485 528 InterPro IPR018392 LysM domain
350 393 SMART SM00257 LysM_2
350 393 InterPro IPR018392 LysM domain
420 462 SUPERFAMILY SSF54106 LysM domain
420 462 InterPro IPR036779 LysM domain superfamily
419 462 ProSiteProfiles PS51782 LysM domain profile.
419 462 InterPro IPR018392 LysM domain
349 392 CDD cd00118 LysM
1 32 ProSiteProfiles PS51257 Prokaryotic membrane lipoprotein lipid attachment site profile.
483 529 Gene3D G3DSA:3.10.350.10 LysM domain
483 529 InterPro IPR036779 LysM domain superfamily
419 462 CDD cd00118 LysM
483 529 FunFam G3DSA:3.10.350.10:FF:000012 Membrane-bound lytic murein transglycosylase D

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

Loading 3D structure...

Legend High Medium Low

Structural evidence

3 + 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 8RHE
X-ray 1.95 Å A,B
59.6% 76-393
PDBe RCSB PDBj File
Viewing
PDB 8RHF
X-ray 1.95 Å A,B
59.6% 76-393
PDBe RCSB PDBj File
Loaded
PDB 8RHI
X-ray 1.98 Å A,B
59.6% 76-393
PDBe RCSB PDBj File
Loaded
AlphaFold PA1812
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 0.703

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 2.49 0.069
2 1.76 0.032
3 1.64 0.027

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.

2 records

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
BUL
6FCQ
Q9HZI6 551.5 Da LogP -5.13 TPSA 267.3 3 viol. ✓ Clean CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@H]1O[C@H]2…

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.