Protein profile

KP13_01110

Cell division protease ftsH

Genome: KpKP13

Gene: ftsH AHE42496.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GTR0

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Amino acids 644

Annotations 10

Features 43

PDB binders 2

Druggability 0.765

Overview

Basic information about this protein and its source genome.

Accession: KP13_01110
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: ftsH AHE42496.1
Status: annotated
Amino acids: 644
Structure source: AlphaFold + ColabFold

3.4.24.-

GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. GO:0008270 Binding to a zinc ion (Zn). GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 58.824
Human E-value: 6.65e-46
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 97.981
DEG E-value: 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 83.05

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 0.765

Structure A0A0H3GTR0

Pocket Pocket 22

P2Rank 0.839

Structure A0A0H3GTR0

Pocket Pocket 1

ColabFold model

FPocket 0.652 · Pocket 12

P2Rank 0.895 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2825 / 4744 genomes with a hit

Normalized 0.595

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)

3.4.24.-

Gene Ontology (GO)

GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0008270 Binding to a zinc ion (Zn).
GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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:0030163 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
5	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
322	396	FunFam	G3DSA:1.10.8.60:FF:000001	ATP-dependent zinc metalloprotease FtsH
396	599	Gene3D	G3DSA:1.20.58.760	Peptidase M41
396	599	InterPro	IPR037219	Peptidase M41-like
149	319	CDD	cd19501	RecA-like_FtsH
184	323	SMART	SM00382	AAA_5
184	323	InterPro	IPR003593	AAA+ ATPase domain
343	387	Pfam	PF17862	AAA+ lid domain
343	387	InterPro	IPR041569	AAA ATPase, AAA+ lid domain
3	616	Hamap	MF_01458	ATP-dependent zinc metalloprotease FtsH [ftsH].
3	616	InterPro	IPR005936	ATP-dependent zinc metalloprotease, FtsH
322	395	Gene3D	G3DSA:1.10.8.60	-
5	93	Pfam	PF06480	FtsH Extracellular
5	93	InterPro	IPR011546	Peptidase M41, FtsH extracellular
22	97	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
401	591	Pfam	PF01434	Peptidase family M41
401	591	InterPro	IPR000642	Peptidase M41
1	21	SignalP_EUK	SignalP-noTM	SignalP-noTM
141	391	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
141	391	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
138	320	FunFam	G3DSA:3.40.50.300:FF:000001	ATP-dependent zinc metalloprotease FtsH
24	98	Gene3D	G3DSA:3.30.720.210	-
5	24	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
97	119	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
39	595	PANTHER	PTHR23076	METALLOPROTEASE M41 FTSH
17	21	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
9	589	NCBIfam	TIGR01241	ATP-dependent zinc metalloprotease FtsH
9	589	InterPro	IPR005936	ATP-dependent zinc metalloprotease, FtsH
291	309	ProSitePatterns	PS00674	AAA-protein family signature.
291	309	InterPro	IPR003960	ATPase, AAA-type, conserved site
98	119	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
141	320	Gene3D	G3DSA:3.40.50.300	-
141	320	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
120	644	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
397	598	FunFam	G3DSA:1.20.58.760:FF:000001	ATP-dependent zinc metalloprotease FtsH
1	21	Phobius	SIGNAL_PEPTIDE	Signal peptide region
402	602	SUPERFAMILY	SSF140990	FtsH protease domain-like
402	602	InterPro	IPR037219	Peptidase M41-like
24	98	FunFam	G3DSA:3.30.720.210:FF:000001	ATP-dependent zinc metalloprotease FtsH
592	644	MobiDBLite	mobidb-lite	consensus disorder prediction
188	320	Pfam	PF00004	ATPase family associated with various cellular activities (AAA)
188	320	InterPro	IPR003959	ATPase, AAA-type, core
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.

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_A0A0H3GTR0	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01110	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
22				0.765
24				0.707

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	14.42	0.722
2	5.82	0.284
3	2.49	0.069
4	2.4	0.064

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
12				0.652
39				0.399
38				0.362

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	17.34	0.801
2	7.43	0.39
3	2.88	0.091
4	1.68	0.029
5	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.

52 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
ANP	5MPB	P33299	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
NHX	3KDS	Q9WZ49	456.5 Da LogP 1.41 TPSA 150.6	✓ Ro5	✓ Clean	`C[C@@H](C(=O)N)NC(=O)[C@H](Cc1ccc2ccccc2c1)NC(=…`

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
ZINC11688557	1.000	456.5 Da LogP 1.41 TPSA 150.6	✓ Ro5	✓ Clean	`CC(C)C[C@@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc…`
ZINC3786507	1.000	456.5 Da LogP 1.41 TPSA 150.6	✓ Ro5	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc2…`
ZINC13907320	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc…`
ZINC3813502	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc2…`
ZINC44681840	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@@H](CC(=O)NO)C(=O)N[C@H](Cc1ccc2ccccc2…`
ZINC44681843	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@H](Cc1ccc2ccccc2c…`
ZINC95911029	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@H](Cc1ccc2ccccc2c…`
ZINC98183634	0.828	499.6 Da LogP 1.00 TPSA 162.7	1 viol.	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc2…`
ZINC12360002	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC35850116	0.729	456.5 Da LogP 1.41 TPSA 150.6	✓ Ro5	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1cccc2ccccc…`
ZINC4096224	0.729	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC1560408734	0.708	498.6 Da LogP 1.17 TPSA 162.7	1 viol.	✓ Clean	`C[C](NC(=O)[C@@H](Cc1ccc2ccccc2c1)NC(=O)[C@H](C…`
ZINC1560408735	0.708	498.6 Da LogP 1.17 TPSA 162.7	1 viol.	✓ Clean	`C[C](NC(=O)[C@@H](Cc1ccc2ccccc2c1)NC(=O)[C@@H](…`
ZINC31475423	0.703	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC1532902	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC117292468	0.697	499.6 Da LogP 1.09 TPSA 167.8	✓ Ro5	✓ Clean	`CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc2…`
ZINC642881691	0.697	499.6 Da LogP 1.09 TPSA 167.8	✓ Ro5	✓ Clean	`CC(C)C[C@@H](CC(=O)NO)C(=O)N[C@@H](Cc1ccc2ccccc…`
ZINC13527614	0.694	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=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.