Overview
Basic information about this protein and its source genome.
- Accession
- KP13_03929
- Gene
- AHE45325.1
- Status
- annotated
- Amino acids
- 427
- Structure source
- AlphaFold + ColabFold
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
- Periplasmic
- ColabFold pLDDT
- 91.07
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
8- GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
- GO:0004601 Catalysis of the reaction: a reduced substrate + ROOH = an oxidized substrate + ROH + H2O.
- GO:0033212 The directed movement of iron ions from outside of a cell into the cytoplasmic compartment. This may occur via transport across the plasma membrane or via endocytosis.
- GO:0030313 An envelope that surrounds a bacterial cell and includes the cytoplasmic membrane and everything external, encompassing the periplasmic space, cell wall, and outer membrane if present.
- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
- GO:0004325 Catalysis of the reaction: heme B (protoheme) + H+ = Fe(2+) + protoporphyrin IX.
- GO:0046872 Binding to a metal ion.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 34 | ProSiteProfiles | PS51257 | Prokaryotic membrane lipoprotein lipid attachment site profile. |
| 62 | 419 | ProSiteProfiles | PS51404 | DyP-type peroxidase family. |
| 62 | 419 | InterPro | IPR006314 | Dyp-type peroxidase |
| 13 | 39 | NCBIfam | TIGR01409 | twin-arginine translocation signal domain |
| 13 | 39 | InterPro | IPR019546 | Twin-arginine translocation pathway, signal sequence, bacterial/archaeal |
| 40 | 427 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 7 | 426 | NCBIfam | TIGR01412 | iron uptake transporter deferrochelatase/peroxidase subunit |
| 7 | 426 | InterPro | IPR006313 | Deferrochelatase |
| 65 | 413 | Pfam | PF04261 | Dyp-type peroxidase family |
| 65 | 413 | InterPro | IPR006314 | Dyp-type peroxidase |
| 1 | 39 | ProSiteProfiles | PS51318 | Twin arginine translocation (Tat) signal profile. |
| 1 | 39 | InterPro | IPR006311 | Twin-arginine translocation pathway, signal sequence |
| 1 | 39 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 1 | 19 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 57 | 415 | PANTHER | PTHR30521 | DEFERROCHELATASE/PEROXIDASE |
| 57 | 415 | InterPro | IPR006314 | Dyp-type peroxidase |
| 20 | 31 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 39 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 58 | 419 | SUPERFAMILY | SSF54909 | Dimeric alpha+beta barrel |
| 58 | 419 | InterPro | IPR011008 | Dimeric alpha-beta barrel |
| 65 | 413 | NCBIfam | TIGR01413 | Dyp-type peroxidase |
| 32 | 39 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-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.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GMM5
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_03929
|
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 |
|---|---|---|---|---|---|---|---|
| 4 | 0.976 |
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 | 38.38 | 0.96 |
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 | 0.984 |
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 | 36.79 | 0.956 | ||||||
| 2 | 2.42 | 0.065 |
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.
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 |
|---|---|---|---|---|---|---|
| OXY | A0A6I8WFL8 | 32.0 Da LogP 0.07 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
O=O
|
|
| PEO | Q9RKQ2 | 34.0 Da LogP 0.02 TPSA 40.5 | ✓ Ro5 | ✓ Clean |
OO
|
|
| PP9 | P31545 | 562.7 Da LogP 7.50 TPSA 132.0 | 2 viol. | ✓ Clean |
Cc1c2\cc\3/nc(\cc/4\c(c(/c(/[nH]4)c/c5n/c(c\c(c…
|
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.