Protein profile

PA4751

cell division protein FtsH

Genome: NC_002516.2

Gene: PA4751 ftsH Structure source: AlphaFold UniProt Q9HV48

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Amino acids 639

Annotations 12

Features 44

PDB binders 2

Druggability 0.809

Overview

Basic information about this protein and its source genome.

Accession: PA4751
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4751 ftsH
Status: annotated
Amino acids: 639
Structure source: AlphaFold

3.4.24.-

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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. 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: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:0008270 Binding to a zinc ion (Zn).

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 57.471
Human E-value: 2.24e-27
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 0.809

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)

3.4.24.-

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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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: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:0008270 Binding to a zinc ion (Zn).
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:0071236 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
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.
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

44 records

Show feature table

Start	End	DB	Term	Name
324	398	FunFam	G3DSA:1.10.8.60:FF:000001	ATP-dependent zinc metalloprotease FtsH
145	393	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
145	393	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
5	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
324	397	Gene3D	G3DSA:1.10.8.60	-
1	26	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
29	97	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
399	601	FunFam	G3DSA:1.20.58.760:FF:000001	ATP-dependent zinc metalloprotease FtsH
98	120	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
121	639	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
596	639	MobiDBLite	mobidb-lite	consensus disorder prediction
98	120	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
3	625	Hamap	MF_01458	ATP-dependent zinc metalloprotease FtsH [ftsH].
3	625	InterPro	IPR005936	ATP-dependent zinc metalloprotease, FtsH
190	322	Pfam	PF00004	ATPase family associated with various cellular activities (AAA)
190	322	InterPro	IPR003959	ATPase, AAA-type, core
22	99	FunFam	G3DSA:3.30.720.210:FF:000004	ATP-dependent zinc metalloprotease FtsH
1	21	SignalP_EUK	SignalP-noTM	SignalP-noTM
151	321	CDD	cd19501	RecA-like_FtsH
293	311	ProSitePatterns	PS00674	AAA-protein family signature.
293	311	InterPro	IPR003960	ATPase, AAA-type, conserved site
22	99	Gene3D	G3DSA:3.30.720.210	-
140	322	FunFam	G3DSA:3.40.50.300:FF:000001	ATP-dependent zinc metalloprotease FtsH
403	595	Pfam	PF01434	Peptidase family M41
403	595	InterPro	IPR000642	Peptidase M41
143	322	Gene3D	G3DSA:3.40.50.300	-
143	322	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
5	24	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
5	91	Pfam	PF06480	FtsH Extracellular
5	91	InterPro	IPR011546	Peptidase M41, FtsH extracellular
398	600	Gene3D	G3DSA:1.20.58.760	Peptidase M41
398	600	InterPro	IPR037219	Peptidase M41-like
404	606	SUPERFAMILY	SSF140990	FtsH protease domain-like
404	606	InterPro	IPR037219	Peptidase M41-like
17	28	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	28	Phobius	SIGNAL_PEPTIDE	Signal peptide region
61	597	PANTHER	PTHR23076	METALLOPROTEASE M41 FTSH
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
186	325	SMART	SM00382	AAA_5
186	325	InterPro	IPR003593	AAA+ ATPase domain
8	592	NCBIfam	TIGR01241	ATP-dependent zinc metalloprotease FtsH
8	592	InterPro	IPR005936	ATP-dependent zinc metalloprotease, FtsH
346	388	Pfam	PF17862	AAA+ lid domain
346	388	InterPro	IPR041569	AAA ATPase, AAA+ lid domain

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

0 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA4751	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				0.562
2				0.515

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.