Target candidate with partial support; inspect missing evidence before prioritizing.
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
- 1.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- Y
- DEG identity (%)
- 93.269 Higher values support similarity to known essential genes.
- DEG E-value
- 1.0400000000000001e-70 Smaller values mean stronger essential-gene similarity.
Localization
- Localization
- Unknown
Structure confidence
- ColabFold pLDDT
- 94.62 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
PDB experimental structureThe 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
Structure
Sequence
Primary amino-acid sequence viewer.
MTNRLELSGIICRTPLRKVSPSGIPHCQFVLEHRSVQEEAGFHRQAWCQMPVIISGHENQAITHSITVGSAVTVRGFISCHKAKNGLSKMVLHAEQIELIDSGD
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
3- GO:0030894 A multi-component enzymatic machine at the replication fork which mediates DNA replication. Includes DNA primase, one or more DNA polymerases, DNA helicases, and other proteins.
- GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
- GO:0003697 Binding to single-stranded DNA.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 2 | 100 | Hamap | MF_00720 | Primosomal replication protein N [priB]. |
| 2 | 100 | InterPro | IPR023646 | Primosomal replication protein PriB |
| 3 | 99 | NCBIfam | TIGR04418 | primosomal replication protein N |
| 3 | 99 | InterPro | IPR023646 | Primosomal replication protein PriB |
| 1 | 103 | SUPERFAMILY | SSF50249 | Nucleic acid-binding proteins |
| 1 | 103 | InterPro | IPR012340 | Nucleic acid-binding, OB-fold |
| 1 | 104 | FunFam | G3DSA:2.40.50.140:FF:000077 | Primosomal replication protein N |
| 3 | 88 | Pfam | PF00436 | Single-strand binding protein family |
| 3 | 88 | InterPro | IPR000424 | Primosome PriB/single-strand DNA-binding |
| 1 | 101 | PIRSF | PIRSF003135 | Primosomal_n |
| 1 | 101 | InterPro | IPR023646 | Primosomal replication protein PriB |
| 1 | 101 | ProSiteProfiles | PS50935 | Single-strand binding (SSB) domain profile. |
| 1 | 101 | InterPro | IPR000424 | Primosome PriB/single-strand DNA-binding |
| 1 | 104 | Gene3D | G3DSA:2.40.50.140 | - |
| 1 | 104 | InterPro | IPR012340 | Nucleic acid-binding, OB-fold |
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 · 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
All structural evidence
Structural evidence
1 + 1Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.
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.
Only proposed virtual-screening candidates are available for this target.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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.
No PDB ligands found through similar proteins.
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).
| Ligand | Tanimoto | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| ZINC5131766 ZINC | 0.538 | 224.3 Da LogP -1.26 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)O
|
| ZINC1730666 ZINC | 0.524 | 208.2 Da LogP -1.46 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CSC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1730667 ZINC | 0.524 | 208.2 Da LogP -1.46 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CSC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1730669 ZINC | 0.524 | 208.2 Da LogP -1.46 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CSC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC3055005 ZINC | 0.524 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O
|
| ZINC3055007 ZINC | 0.524 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC3055010 ZINC | 0.524 | 204.2 Da LogP -0.63 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1555366 ZINC | 0.500 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1555367 ZINC | 0.500 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1555369 ZINC | 0.500 | 232.3 Da LogP 0.15 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1720127 ZINC | 0.500 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O
|
| ZINC1720128 ZINC | 0.500 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC1720130 ZINC | 0.500 | 218.3 Da LogP -0.24 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O
|
| ZINC3623257 ZINC | 0.500 | 202.2 Da LogP -0.85 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](C/C=C/C[C@@H](N)C(=O)O)C(=O)O
|
| ZINC40439568 ZINC | 0.500 | 208.2 Da LogP -2.19 TPSA 112.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CS)C(=O)N[C@@H](CO)C(=O)O
|
| ZINC4580672 ZINC | 0.500 | 202.2 Da LogP -0.85 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](C/C=C/C[C@H](N)C(=O)O)C(=O)O
|
| ZINC4580676 ZINC | 0.500 | 202.2 Da LogP -0.85 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](C/C=C/C[C@@H](N)C(=O)O)C(=O)O
|
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.