Protein profile

KP13_00822

Membrane-bound lytic murein transglycosylase F

Genome: KpKP13

Gene: AHE43186.1 mltF Structure source: AlphaFold + ColabFold UniProt A0A0H3GW83

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Amino acids 538

Annotations 9

Features 25

PDB binders 1

Druggability 0.948

Overview

Basic information about this protein and its source genome.

Accession: KP13_00822
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43186.1 mltF
Status: annotated
Amino acids: 538
Structure source: AlphaFold + ColabFold

4.2.2.n1

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0016837 Catalysis of the cleavage of a carbon-oxygen bond by the elimination of an alcohol from a polysaccharide. 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. GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures. GO:0016998 The chemical reactions and pathways resulting in the breakdown of macromolecules that form part of a cell wall.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 87.07

Selected Druggability evidence

AlphaFold / UniProt model

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 0.948

Structure A0A0H3GW83

Pocket Pocket 8

P2Rank 0.873

Structure A0A0H3GW83

Pocket Pocket 1

ColabFold model

FPocket 0.503 · Pocket 36

P2Rank 0.842 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 115 / 4744 genomes with a hit

Normalized 0.024

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

4.2.2.n1

Gene Ontology (GO)

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0016837 Catalysis of the cleavage of a carbon-oxygen bond by the elimination of an alcohol from a polysaccharide.
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.
GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.
GO:0016998 The chemical reactions and pathways resulting in the breakdown of macromolecules that 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:0009253 The chemical reactions and pathways resulting in the breakdown 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
71	296	SMART	SM00062	AABind_6
71	296	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
33	55	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
33	53	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
156	252	Gene3D	G3DSA:3.40.190.10	-
33	429	PANTHER	PTHR35936	MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F
298	479	Gene3D	G3DSA:1.10.530.10	-
54	538	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
156	252	FunFam	G3DSA:3.40.190.10:FF:000051	Membrane-bound lytic murein transglycosylase F
68	296	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II
66	290	Gene3D	G3DSA:3.40.190.10	-
337	365	ProSitePatterns	PS00922	Prokaryotic transglycosylases signature.
337	365	InterPro	IPR000189	Prokaryotic transglycosylase, active site
273	468	SUPERFAMILY	SSF53955	Lysozyme-like
273	468	InterPro	IPR023346	Lysozyme-like domain superfamily
70	294	CDD	cd01009	PBP2_YfhD_N
32	499	Hamap	MF_02016	Membrane-bound lytic murein transglycosylase F [mltF].
32	499	InterPro	IPR023703	Membrane-bound lytic murein transglycosylase F
1	32	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
299	479	FunFam	G3DSA:1.10.530.10:FF:000003	Membrane-bound lytic murein transglycosylase F
78	295	Pfam	PF00497	Bacterial extracellular solute-binding proteins, family 3
78	295	InterPro	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF
322	479	CDD	cd13403	MLTF-like
324	430	Pfam	PF01464	Transglycosylase SLT domain
324	430	InterPro	IPR008258	Transglycosylase SLT domain 1

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

0 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GW83	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00822	ColabFold	—	—	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
8				0.948

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	19.06	0.834
2	14.07	0.71
3	2.69	0.08
4	1.36	0.016
5	1.04	0.006

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
36				0.503

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	32.71	0.944
2	1.82	0.035
3	1.55	0.023
4	1.31	0.014
5	0.89	0.004

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.

51 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
6X4	5AA4	A0A1I9GEN8	489.6 Da LogP -3.89 TPSA 244.7	1 viol.	✓ Clean	`C[C@H](C(=O)N)NC(=O)C(CCCC[NH3+])NC(=O)CC[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).

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
ZINC15722130	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@@H](CCCCN)C(=O)…`
ZINC255987061	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC255987062	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC255987063	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC255987064	0.582	488.5 Da LogP -2.61 TPSA 243.0	1 viol.	✓ Clean	`C[C@H](N)C(=O)N[C@H](CCC(=O)N[C@H](CCCCN)C(=O)N…`
ZINC64219359	0.565	202.3 Da LogP -0.41 TPSA 106.4	✓ Ro5	✓ Clean	`CC(C)[C@H](C(=O)[C@@H](C)N)[C@H](N)C(=O)O`
ZINC64219360	0.565	202.3 Da LogP -0.41 TPSA 106.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](C(=O)[C@@H](C)N)[C@H](N)C(=O)O`
ZINC79670384	0.565	202.3 Da LogP -0.41 TPSA 106.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](C(=O)[C@H](C)N)[C@H](N)C(=O)O`
ZINC79670387	0.565	202.3 Da LogP -0.41 TPSA 106.4	✓ Ro5	✓ Clean	`CC(C)[C@H](C(=O)[C@H](C)N)[C@H](N)C(=O)O`
ZINC2516116	0.559	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC4545887	0.559	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC4545888	0.559	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCC(=O)NCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC4545889	0.559	275.3 Da LogP -1.12 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=O)CC[C@@H](N)C(=O)O)C(=O)O`
ZINC50027904	0.559	261.3 Da LogP -1.51 TPSA 155.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC3055005	0.556	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007	0.556	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010	0.556	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC100017163	0.553	213.3 Da LogP 0.71 TPSA 99.2	✓ Ro5	✓ Clean	`C/C=C/CC(=N)NCCC[C@H](N)C(=O)O`
ZINC19796052	0.553	219.2 Da LogP -1.73 TPSA 156.9	✓ Ro5	✓ Clean	`N/C(=N\[N+](=O)[O-])NCCC[C@H](N)C(=O)O`
ZINC21982226	0.553	219.2 Da LogP -1.73 TPSA 156.9	✓ Ro5	✓ Clean	`N/C(=N\[N+](=O)[O-])NCCC[C@@H](N)C(=O)O`
ZINC5113209	0.548	275.3 Da LogP -0.26 TPSA 138.7	✓ Ro5	✓ Clean	`N[C@@H](CCCCNCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC13545298	0.543	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCC(=O)NCCCC[C@H](N)C(=O)O`
ZINC6360447	0.543	222.3 Da LogP 0.37 TPSA 75.3	✓ Ro5	✓ Clean	`N[C@H](CCCCNC(=S)S)C(=O)O`
ZINC5131766	0.538	224.3 Da LogP -1.26 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)O`
ZINC1555366	0.536	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1555367	0.536	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1555369	0.536	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720127	0.536	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1720128	0.536	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720130	0.536	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC13529436	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N1CCCCCC1`
ZINC19502834	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@@H](N)C(=O)N1CCCCCC1`
ZINC19502836	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](N)C(=O)N1CCCCCC1`
ZINC19502838	0.533	212.3 Da LogP 1.76 TPSA 46.3	✓ Ro5	✓ Clean	`CC[C@@H](C)[C@H](N)C(=O)N1CCCCCC1`
ZINC1608689	0.528	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCNC(=O)CC[C@H](N)C(=O)O`
ZINC1737889	0.528	245.3 Da LogP -0.33 TPSA 118.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)NCCCC[C@H](N)C(=O)O`
ZINC1737892	0.528	245.3 Da LogP -0.33 TPSA 118.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](N)C(=O)NCCCC[C@H](N)C(=O)O`
ZINC1737894	0.528	245.3 Da LogP -0.33 TPSA 118.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)NCCCC[C@@H](N)C(=O)O`
ZINC1737898	0.528	245.3 Da LogP -0.33 TPSA 118.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](N)C(=O)NCCCC[C@@H](N)C(=O)O`
ZINC2045835	0.528	202.3 Da LogP 0.09 TPSA 92.4	✓ Ro5	✓ Clean	`CCCCNC(=O)CC[C@@H](N)C(=O)O`
ZINC1529646	0.526	290.3 Da LogP -1.78 TPSA 185.8	1 viol.	✓ Clean	`N=C(NCCC[C@H](N)C(=O)O)N[C@@H](CC(=O)O)C(=O)O`
ZINC2028776	0.526	307.6 Da LogP 1.27 TPSA 101.6	✓ Ro5	✓ Clean	`N[C@@H](CCCNC(=O)OCC(Cl)(Cl)Cl)C(=O)O`
ZINC2028780	0.526	307.6 Da LogP 1.27 TPSA 101.6	✓ Ro5	✓ Clean	`N[C@H](CCCNC(=O)OCC(Cl)(Cl)Cl)C(=O)O`
ZINC2043460	0.526	214.3 Da LogP -0.52 TPSA 111.2	✓ Ro5	✓ Clean	`C=CCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC1848346	0.520	216.3 Da LogP 0.20 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)N[C@H](C(=O)O)C(C)C`
ZINC1848348	0.520	216.3 Da LogP 0.20 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)[C@H](N)C(C)C)C(=O)O`
ZINC1848350	0.520	216.3 Da LogP 0.20 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)N[C@@H](C(=O)O)C(C)C`
ZINC1848352	0.520	216.3 Da LogP 0.20 TPSA 92.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](N)C(=O)N[C@@H](C(=O)O)C(C)C`
ZINC11959315	0.516	213.3 Da LogP 0.13 TPSA 49.6	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)N1CCN(C)CC1`
ZINC19504599	0.516	213.3 Da LogP 0.13 TPSA 49.6	✓ Ro5	✓ Clean	`CC[C@H](C)[C@@H](N)C(=O)N1CCN(C)CC1`

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.