Protein profile

KP13_05304

Thiol:disulfide interchange protein dsbE

Genome: KpKP13

Gene: dsbE AHE44178.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GTZ7
Export view
Amino acids 184
Annotations 6
Features 21
PDB binders 0
Druggability 0.366

Overview

Basic information about this protein and its source genome.

Accession
KP13_05304
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
dsbE AHE44178.1
Status
annotated
Amino acids
184
Structure source
AlphaFold + ColabFold
GO
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0015036 Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds. GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. GO:0017004 The aggregation, arrangement and bonding together of a cytochrome complex. A cytochrome complex is a protein complex in which at least one of the proteins is a cytochrome, i.e. a heme-containing protein involved in catalysis of redox reactions. 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:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.

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
CytoplasmicMembrane
ColabFold pLDDT
92.25

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 0.366
Structure A0A0H3GTZ7
Pocket Pocket 11
P2Rank
Structure A0A0H3GTZ7
Pocket No pockets
ColabFold model
FPocket 0.65 · Pocket 14
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 113 / 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.

6 GO

Gene Ontology (GO)

6
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0015036 Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds.
  • GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
  • GO:0017004 The aggregation, arrangement and bonding together of a cytochrome complex. A cytochrome complex is a protein complex in which at least one of the proteins is a cytochrome, i.e. a heme-containing protein involved in catalysis of redox reactions.
  • 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:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.

Sequence Features

Domain/signature hits from InterPro and related databases.

21 records
Show feature table
Start End DB Term Name
39 181 ProSiteProfiles PS51352 Thioredoxin domain profile.
39 181 InterPro IPR013766 Thioredoxin domain
5 16 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
5 24 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
6 177 NCBIfam TIGR00385 DsbE family thiol:disulfide interchange protein
6 177 InterPro IPR004799 Periplasmic protein thiol:disulphide oxidoreductase DsbE
21 182 Gene3D G3DSA:3.40.30.10 Glutaredoxin
17 21 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
43 169 CDD cd03010 TlpA_like_DsbE
43 169 InterPro IPR004799 Periplasmic protein thiol:disulphide oxidoreductase DsbE
22 184 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 30 SignalP_EUK SignalP-noTM SignalP-noTM
1 21 Phobius SIGNAL_PEPTIDE Signal peptide region
42 164 Pfam PF08534 Redoxin
42 164 InterPro IPR013740 Redoxin
72 90 ProSitePatterns PS00194 Thioredoxin family active site.
72 90 InterPro IPR017937 Thioredoxin, conserved site
46 178 SUPERFAMILY SSF52833 Thioredoxin-like
46 178 InterPro IPR036249 Thioredoxin-like superfamily
28 174 PANTHER PTHR42852 THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE
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.

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_A0A0H3GTZ7
AlphaFold — — full sequence — Viewing
ColabFold KP13_05304
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
11 0.366