Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: KP13_00577
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: hslV AHE47052.1
Status: annotated
Amino acids: 176
Structure source: AlphaFold + ColabFold

EC

3.4.25.2

GO

GO:0004298 Catalysis of the hydrolysis of internal peptide bonds in a polypeptide chain by a mechanism in which the hydroxyl group of a threonine residue at the active center acts as a nucleophile. GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. GO:0051603 OBSOLETE. The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. GO:0009376 A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. GO:0005839 A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex. GO:0046872 Binding to a metal ion.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 70.286
DEG E-value: 8.1499999999999995e-84
Localization: Cytoplasmic
ColabFold pLDDT: 95.88

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 0.059

Structure A0A0H3GLF6

Pocket Pocket 2

P2Rank 0.138

Structure A0A0H3GLF6

Pocket Pocket 1

ColabFold model

FPocket 0.114 · Pocket 3

P2Rank 0.112 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 876 / 4744 genomes with a hit

Normalized 0.185

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

3.4.25.2

Gene Ontology (GO)

6

GO:0004298 Catalysis of the hydrolysis of internal peptide bonds in a polypeptide chain by a mechanism in which the hydroxyl group of a threonine residue at the active center acts as a nucleophile.
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0051603 OBSOLETE. The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
GO:0009376 A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer.
GO:0005839 A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex.
GO:0046872 Binding to a metal ion.

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records

Show feature table

Start	End	DB	Term	Name
1	172	SUPERFAMILY	SSF56235	N-terminal nucleophile aminohydrolases (Ntn hydrolases)
1	172	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
1	175	PIRSF	PIRSF039093	HslV
1	175	InterPro	IPR022281	ATP-dependent protease, HslV subunit
1	173	FunFam	G3DSA:3.60.20.10:FF:000002	ATP-dependent protease subunit HslV
1	173	Gene3D	G3DSA:3.60.20.10	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
1	173	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
2	172	PANTHER	PTHR32194	METALLOPROTEASE TLDD
2	172	InterPro	IPR023333	Proteasome B-type subunit
1	172	ProSiteProfiles	PS51476	Proteasome beta-type subunit profile.
1	172	InterPro	IPR023333	Proteasome B-type subunit
1	172	Hamap	MF_00248	ATP-dependent protease subunit HslV [hslV].
1	172	InterPro	IPR022281	ATP-dependent protease, HslV subunit
2	168	Pfam	PF00227	Proteasome subunit
2	168	InterPro	IPR001353	Proteasome, subunit alpha/beta
2	172	NCBIfam	TIGR03692	HslU--HslV peptidase proteolytic subunit
2	172	InterPro	IPR022281	ATP-dependent protease, HslV subunit
2	172	CDD	cd01913	protease_HslV

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_A0A0H3GLF6	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00577	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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				2.19	0.052

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.

1 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
LVS	1KYI	P43772	722.6 Da LogP 3.60 TPSA 184.8	1 viol.	✓ Clean	`CC(C)C[C@@H](C=CS(=O)(=O)C)NC(=O)[C@H](CC(C)C)N…`

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).

No virtual-screening candidates for this protein.

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.

KP13_00577