Protein profile

VK055_4642

fe-S protein assembly co-chaperone

Genome: KpATCC43816

Gene: AIK83176.1 hscB Structure source: AlphaFold + ColabFold UniProt A0A0H3GTL7
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Amino acids 171
Annotations 6
Features 27
PDB binders 0
Druggability 0.357

Overview

Basic information about this protein and its source genome.

Accession
VK055_4642
Assembly
Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene
AIK83176.1 hscB
Status
annotated
Amino acids
171
Structure source
AlphaFold + ColabFold
GO
GO:0001671 Binds to and increases the activity of an ATP hydrolysis activity. GO:0044571 The incorporation of two iron atoms and two sulfur atoms into an iron-sulfur cluster. GO:0051087 Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. GO:0051259 The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer. GO:1990230 A protein complex capable of catalyzing the transfer of an iron-sulfur (Fe-S) cluster from one compound (donor) to another (acceptor), which may be a target protein or another Fe-S assembly complex. In humans, it consists of HSPA9, HSCB, GLRX5, ABCB7 and GFER. GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
40.278
Human E-value
8.01e-09
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
85.38
DEG E-value
3.89e-104
Localization
Cytoplasmic
ColabFold pLDDT
92.11

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 0.357
Structure A0A0H3GTL7
Pocket Pocket 15
P2Rank
Structure A0A0H3GTL7
Pocket No pockets
ColabFold model
FPocket 0.059 · Pocket 7
P2Rank 0.003 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 103 / 4744 genomes with a hit
Normalized 0.022

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • GO:0001671 Binds to and increases the activity of an ATP hydrolysis activity.
  • GO:0044571 The incorporation of two iron atoms and two sulfur atoms into an iron-sulfur cluster.
  • GO:0051087 Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
  • GO:0051259 The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
  • GO:1990230 A protein complex capable of catalyzing the transfer of an iron-sulfur (Fe-S) cluster from one compound (donor) to another (acceptor), which may be a target protein or another Fe-S assembly complex. In humans, it consists of HSPA9, HSCB, GLRX5, ABCB7 and GFER.
  • GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records
Show feature table
Start End DB Term Name
1 169 Hamap MF_00682 Co-chaperone protein HscB [hscB].
1 169 InterPro IPR004640 Co-chaperone Hsc20
80 170 FunFam G3DSA:1.20.1280.20:FF:000001 Co-chaperone protein HscB
88 161 Pfam PF07743 HSCB C-terminal oligomerisation domain
88 161 InterPro IPR009073 Co-chaperone HscB, C-terminal oligomerisation domain
2 74 ProSiteProfiles PS50076 dnaJ domain profile.
2 74 InterPro IPR001623 DnaJ domain
2 163 PANTHER PTHR14021 IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB
2 163 InterPro IPR004640 Co-chaperone Hsc20
2 61 CDD cd06257 DnaJ
2 61 InterPro IPR001623 DnaJ domain
13 168 NCBIfam TIGR00714 Fe-S protein assembly co-chaperone HscB
13 168 InterPro IPR004640 Co-chaperone Hsc20
1 79 Gene3D G3DSA:1.10.287.110 DnaJ domain
1 79 InterPro IPR036869 Chaperone J-domain superfamily
80 170 Gene3D G3DSA:1.20.1280.20 -
80 170 InterPro IPR036386 HscB, C-terminal domain superfamily
1 75 SUPERFAMILY SSF46565 Chaperone J-domain
1 75 InterPro IPR036869 Chaperone J-domain superfamily
154 171 Coils Coil Coil
1 79 FunFam G3DSA:1.10.287.110:FF:000008 Co-chaperone protein HscB
77 170 SUPERFAMILY SSF47144 HSC20 (HSCB), C-terminal oligomerisation domain
77 170 InterPro IPR036386 HscB, C-terminal domain superfamily
1 66 SMART SM00271 dnaj_3
1 66 InterPro IPR001623 DnaJ domain
2 70 Pfam PF00226 DnaJ domain
2 70 InterPro IPR001623 DnaJ domain

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

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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_A0A0H3GTL7
AlphaFold — — full sequence — Viewing
ColabFold VK055_4642
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
15 0.357
8 0.056
2 0.002
1 0.001