Promising target candidate with multiple supporting evidence streams.
Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.
Main supporting evidence
Risks to review
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
- 1.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- N
- DEG identity (%)
- 28.406 Higher values support similarity to known essential genes.
Localization
- Localization
- CytoplasmicMembrane
Structure confidence
- ColabFold pLDDT
- 85.67 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
AlphaFold DB / UniProt modelThe 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.
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.
Sequence
Sequence
Primary amino-acid sequence viewer.
MKCRWQEGNRITLLENGDQYYPALFAAIGRASRRVILESFIWFEDEVGRRLHAVLLEAARRGIQVEVLLDGYGSPDLSDEFVGELTAAGVIFRYYDPRPKLMGMRTNLFRRMHRKIVVIDDTTAFVGGINYSAEHMSDYGPEAKQDYAVQVEGPVVLDILQFELENLPNSETARRWWRRRRHQPEINQTPGEAQALFVWRDNQDHRDDIERHYLKMLTSARREVIIANAYFFPGYRLLHAMRNAARRGVRVKLIVQGEPDIPIVKFGAHLLYHYLVKGGVQIYEYRRRPLHGKVALADDHWATVGSSNLDPLSLSLNLEANLIIHDRVFNQTLRDNLNGLIARDCQRIDKTMLPKRNWWRLGVSVMAFHFLRHFPAWVGWLPAHTPRLARVSPPVQPEIETQDRVESPARDNPL
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
4- GO:0032049 The chemical reactions and pathways resulting in the formation of cardiolipin, 1,3-bis(3-phosphatidyl)glycerol.
- 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:0008808 Catalysis of the reaction: phosphatidylglycerol + phosphatidylglycerol = diphosphatidylglycerol (cardiolipin) + glycerol.
- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 108 | 135 | SMART | SM00155 | pld_4 |
| 108 | 135 | InterPro | IPR001736 | Phospholipase D/Transphosphatidylase |
| 286 | 313 | SMART | SM00155 | pld_4 |
| 286 | 313 | InterPro | IPR001736 | Phospholipase D/Transphosphatidylase |
| 108 | 135 | ProSiteProfiles | PS50035 | Phospholipase D phosphodiesterase active site profile. |
| 7 | 370 | PANTHER | PTHR21248 | CARDIOLIPIN SYNTHASE |
| 202 | 342 | Gene3D | G3DSA:3.30.870.10 | Endonuclease Chain A |
| 286 | 313 | ProSiteProfiles | PS50035 | Phospholipase D phosphodiesterase active site profile. |
| 3 | 194 | FunFam | G3DSA:3.30.870.10:FF:000016 | Cardiolipin synthase B |
| 26 | 154 | Pfam | PF13091 | PLD-like domain |
| 26 | 154 | InterPro | IPR025202 | Phospholipase D-like domain |
| 215 | 338 | Pfam | PF13091 | PLD-like domain |
| 215 | 338 | InterPro | IPR025202 | Phospholipase D-like domain |
| 16 | 167 | CDD | cd09110 | PLDc_CLS_1 |
| 202 | 340 | FunFam | G3DSA:3.30.870.10:FF:000015 | Cardiolipin synthase B |
| 392 | 414 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 198 | 360 | CDD | cd09159 | PLDc_ybhO_like_2 |
| 2 | 384 | Hamap | MF_01917 | Cardiolipin synthase B [clsB]. |
| 2 | 384 | InterPro | IPR030872 | Cardiolipin synthase B |
| 4 | 173 | SUPERFAMILY | SSF56024 | Phospholipase D/nuclease |
| 188 | 359 | SUPERFAMILY | SSF56024 | Phospholipase D/nuclease |
| 3 | 195 | Gene3D | G3DSA:3.30.870.10 | Endonuclease Chain A |
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.
How colors and pocket overlays are used
Pocket details Inspect a specific pocket, or open the full viewer
- Method
- -
- Score
- -
- Visible layer
- -
- Residues
- -
- Pocket properties
- -
Selecting a pocket opens its details and centers the viewer without clearing other active layers. Use Focus this pocket when you want to hide the rest; use Surface for the wider residue environment.
Binding pockets · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Binding pockets · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Residue sets
Binding pockets · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Binding pockets · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Residue sets
All structural evidence
Structural evidence
0 + 2Experimental 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_A0A0H3GQ81
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
VK055_1714
|
ColabFold | — | — | full sequence | — | Loaded |