Protein target profile

KP13_04231

Hydroxylamine reductase

Genome: KpKP13 Gene: hcp AHE45462.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GQL0
Length 561
Pocket druggability 0.994
Direct ligand evidence 0 2 total records
Functional annotation 1 EC 10 GO
Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target
No hit
Gut microbiome similarity
2.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
N
DEG identity (%)
0.0 Higher values support similarity to known essential genes.

Localization

Localization
Cytoplasmic

Structure confidence

ColabFold pLDDT
96.0 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.994
Structure A0A0H3GQL0
Pocket Pocket 1
P2Rank 0.273
Structure A0A0H3GQL0
Pocket Pocket 1
ColabFold model
FPocket 0.996 · Pocket 1
P2Rank 0.326 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 121 / 4744 genomes with a hit
Prevalence 2.6%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

Primary amino-acid sequence viewer.

MYIKYNFKGVTMFCVQCEQTIRTPAGNGCSYAQGMCGKTAETSDLQDLLIASLQGLSAWALKAREYGIIDHQVDSFAPRAFFSTLTNVNFDSPRIVGYARQAIALREALKAQCLAIDASAAVDSPVADLQLVSDDLGELQRQAADYTPNKDKAAIGENILGLRLLCLYGLKGAAAYMEHAHVLGQYDNAIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETTKYGHPTPTQVNVKATEGKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLIGNYGSGWQNQQVEFARFPGPIVMTSNCIIDPTVGAYDDRIWTRSIVGWPGVNHLEGEDFSPVIAQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIFLVGGCDGARGERNYFTDFATSVPDDCLILTLACGKYRFNKLDFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVNDLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFFTPDLLAVLNEKFGLRSVTTVEQDMQQLLSA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

10
  • GO:0016661 Catalysis of an oxidation-reduction (redox) reaction in which a nitrogenous group, excluding NH and NH2 groups, acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • 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:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
  • GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
  • GO:0050418 Catalysis of the reaction: an acceptor + NH4+ + H2O = hydroxylamine + a reduced acceptor + H+.
  • GO:0046872 Binding to a metal ion.
  • GO:0004601 Catalysis of the reaction: a reduced substrate + ROOH = an oxidized substrate + ROH + H2O.
  • GO:0042542 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records
Show feature table
Start End DB Term Name
388 559 Gene3D G3DSA:3.40.50.2030 -
388 559 InterPro IPR016099 Prismane-like, alpha/beta-sandwich
391 559 FunFam G3DSA:3.40.50.2030:FF:000001 Hydroxylamine reductase
243 384 Gene3D G3DSA:3.40.50.2030 -
243 384 InterPro IPR016099 Prismane-like, alpha/beta-sandwich
243 385 FunFam G3DSA:3.40.50.2030:FF:000002 Hydroxylamine reductase
12 560 Hamap MF_00069 Hydroxylamine reductase [hcp].
12 560 InterPro IPR010048 Hydroxylamine reductase
12 155 Gene3D G3DSA:1.20.1270.20 -
12 155 InterPro IPR016100 Prismane, alpha-bundle
12 556 Pfam PF03063 Prismane/CO dehydrogenase family
12 556 InterPro IPR004137 Hydroxylamine reductase/Ni-containing CO dehydrogenase
12 155 FunFam G3DSA:1.20.1270.20:FF:000002 Hydroxylamine reductase
12 559 CDD cd01914 HCP
12 559 InterPro IPR010048 Hydroxylamine reductase
11 559 SUPERFAMILY SSF56821 Prismane protein-like
11 559 InterPro IPR011254 Prismane-like superfamily
160 243 FunFam G3DSA:1.20.1270.20:FF:000001 Hydroxylamine reductase
12 559 NCBIfam TIGR01703 hydroxylamine reductase
7 559 PANTHER PTHR30109 HYDROXYLAMINE REDUCTASE
7 559 InterPro IPR004137 Hydroxylamine reductase/Ni-containing CO dehydrogenase
161 242 Gene3D G3DSA:1.20.1270.20 -
161 242 InterPro IPR016100 Prismane, alpha-bundle
12 561 PIRSF PIRSF000076 HCP
12 561 InterPro IPR010048 Hydroxylamine reductase

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low
How colors and pocket overlays are used
Uniform protein color marks the displayed model as a single molecular object.
Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.
Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.
'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.
'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.
'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.
Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1
0.994
Likely same site as P2Rank 1 7.8 Å 16 shared residues 100% of smaller site
Unusual size
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Surrounding area
Site 2 FPocket #5
0.617
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Surrounding area
Site 3 FPocket #15
0.291
Likely same site as P2Rank 3 1.4 Å 8 shared residues 89% of smaller site
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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1
0.273
Likely same site as FPocket 1 7.8 Å 16 shared residues 100% of smaller site
Show in viewer
Surrounding area
Site 2 P2Rank #2
0.249
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Surrounding area
Site 3 P2Rank #3
0.157
Likely same site as FPocket 15 1.4 Å 8 shared residues 89% of smaller site
Show in viewer
Surrounding area
Site 4 P2Rank #4
0.133
Show in viewer
Surrounding area
Site 5 P2Rank #5
0.093
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Surrounding area
Residue sets
UniProt: Binding site:14-14
UniProt: Binding site:17-17
UniProt: Binding site:260-260
UniProt: Binding site:284-284
UniProt: Binding site:29-29
UniProt: Binding site:328-328
UniProt: Binding site:36-36
UniProt: Binding site:416-416 via persulfide group
UniProt: Binding site:444-444
UniProt: Binding site:469-469
UniProt: Binding site:503-503
UniProt: Binding site:505-505
All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold DB AF_A0A0H3GQL0
AlphaFold DB full sequence Viewing
ColabFold KP13_04231
ColabFold full sequence Loaded

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.

2 records
Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records
Transferred evidence 2 records from similar proteins
Structural ligands 2 0 loaded crystals
Measured bioactivity 0 direct and transferred ChEMBL records
Proposed compounds 0 similarity-based ZINC candidates
Best available ligand signal
FSO PDB via homolog 367.6 Da · LogP 0.43 · TPSA 27.7 Open detail RCSB PDB
XE PDB via homolog Detail RCSB PDB

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
FSO RCSB PDB P31101 367.6 Da LogP 0.43 TPSA 27.7 ✓ Ro5 ✓ Clean O1[Fe]O[Fe]2(O[Fe]3[S@@+]2[Fe]1S3)[S-]
XE RCSB PDB P31101 131.3 Da LogP 0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Xe]

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.