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
- 3.5% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- Y
- DEG identity (%)
- 71.525 Higher values support similarity to known essential genes.
- DEG E-value
- 1.23e-152 Smaller values mean stronger essential-gene similarity.
Structure confidence
- ColabFold pLDDT
- 94.36 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
AlphaFold DB / UniProt modelP2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
MLDNTRLRIAIQKSGRLSEDSRELLSRCGIKVNLHTQRLIALAENMPIDILRVRDDDIPGLVMDGVVDLGIIGENVLEEELLSRRAQGEDPRYFTLRRLDFGGCRLSLATPVDEAWNGPAALDGKRIATSYPHLLKRYLDQKGISFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEANGLREVEVIYRSKACLIQRDGEMADAKQQLIDRLLTRIQGVIQARESKYIMMHAPTERLEEVVALLPGAERPTILPLAGDKQRVAMHMVSSETLFWETMEKLKALGASSILVLPIEKMME
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Subcellular localization
- Localization
- Cytoplasmic
Enzyme Commission (EC)
1Gene Ontology (GO)
5- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
- GO:0003879 Catalysis of the reaction: 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
- GO:0000287 Binding to a magnesium (Mg) ion.
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 200 | 298 | NCBIfam | TIGR03455 | ATP phosphoribosyltransferase, C-terminal domain |
| 200 | 298 | InterPro | IPR013115 | Histidine biosynthesis HisG, C-terminal |
| 6 | 220 | CDD | cd13592 | PBP2_HisGL2 |
| 7 | 221 | Gene3D | G3DSA:3.40.190.10 | - |
| 102 | 191 | Gene3D | G3DSA:3.40.190.10 | - |
| 104 | 191 | FunFam | G3DSA:3.40.190.10:FF:000008 | ATP phosphoribosyltransferase |
| 2 | 298 | PANTHER | PTHR21403 | ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE |
| 2 | 298 | InterPro | IPR001348 | ATP phosphoribosyltransferase HisG |
| 226 | 299 | FunFam | G3DSA:3.30.70.120:FF:000002 | ATP phosphoribosyltransferase |
| 156 | 177 | ProSitePatterns | PS01316 | ATP phosphoribosyltransferase signature. |
| 156 | 177 | InterPro | IPR018198 | ATP phosphoribosyltransferase, conserved site |
| 226 | 299 | Gene3D | G3DSA:3.30.70.120 | - |
| 226 | 299 | InterPro | IPR015867 | Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal |
| 7 | 197 | NCBIfam | TIGR00070 | ATP phosphoribosyltransferase |
| 7 | 197 | InterPro | IPR013820 | ATP phosphoribosyltransferase, catalytic domain |
| 54 | 219 | Pfam | PF01634 | ATP phosphoribosyltransferase |
| 54 | 219 | InterPro | IPR013820 | ATP phosphoribosyltransferase, catalytic domain |
| 226 | 298 | SUPERFAMILY | SSF54913 | GlnB-like |
| 226 | 298 | InterPro | IPR011322 | Nitrogen regulatory PII-like, alpha/beta |
| 6 | 299 | Hamap | MF_00079 | ATP phosphoribosyltransferase [hisG]. |
| 6 | 299 | InterPro | IPR020621 | ATP phosphoribosyltransferase HisG, long form |
| 223 | 296 | Pfam | PF08029 | HisG, C-terminal domain |
| 223 | 296 | InterPro | IPR013115 | Histidine biosynthesis HisG, C-terminal |
| 6 | 224 | SUPERFAMILY | SSF53850 | Periplasmic binding protein-like II |
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 · P2Rank
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Binding pockets · P2Rank
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
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_A0A0H3H0I5
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_03767
|
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.
Structural ligand evidence is 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.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| PRT RCSB PDB | P60757 | 719.3 Da LogP -3.60 TPSA 385.5 | 3 viol. | ✓ Clean |
[H]/N=C\1/c2c(n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O…
|
|
| TIH RCSB PDB | P9WMN1 | 171.2 Da LogP 0.70 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
c1cc(sc1)C[C@@H](C(=O)O)N
|
|
| TLA RCSB PDB | P60757 | 150.1 Da LogP -2.12 TPSA 115.1 | ✓ Ro5 | ✓ Clean |
[C@@H]([C@H](C(=O)O)O)(C(=O)O)O
|
|
| WO4 RCSB PDB | Q02129 | 247.8 Da LogP -2.62 TPSA 80.3 | ✓ Ro5 | ✓ Clean |
[O-][W](=O)(=O)[O-]
|
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 |
|---|---|---|---|---|---|
| ZINC1671208 ZINC | 0.700 | 200.2 Da LogP 1.08 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)C(Cc1cccs1)C(=O)O
|
| ZINC12359024 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O
|
| ZINC13533920 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC1532740 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O
|
| ZINC1549593 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC2013424 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O
|
| ZINC3581021 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC3860635 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC5783661 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O
|
| ZINC6072527 ZINC | 0.692 | 210.1 Da LogP -3.40 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O
|
| ZINC34718738 ZINC | 0.661 | 444.3 Da LogP -1.04 TPSA 206.6 | 2 viol. | ✓ Clean |
O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@H](n2cnc3c(S)…
|
| ZINC34718739 ZINC | 0.661 | 444.3 Da LogP -1.04 TPSA 206.6 | 2 viol. | ✓ Clean |
O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@@H](n2cnc3c(S…
|
| ZINC34718740 ZINC | 0.661 | 444.3 Da LogP -1.04 TPSA 206.6 | 2 viol. | ✓ Clean |
O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@H](n2cnc3c(S)…
|
| ZINC34718741 ZINC | 0.661 | 444.3 Da LogP -1.04 TPSA 206.6 | 2 viol. | ✓ Clean |
O=P(O)(O)O[P@](=O)(O)OC[C@@H]1O[C@@H](n2cnc3c(S…
|
| ZINC13507175 ZINC | 0.656 | 451.2 Da LogP -1.08 TPSA 211.0 | 1 viol. | ✓ Clean |
O=P(O)(O)O[P@](=O)(O)OC[C@H]1O[C@@H](n2cnc3c2nc…
|
| ZINC12360002 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC12360703 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC12503599 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC16546165 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…
|
| ZINC31977053 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…
|
| ZINC4806433 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC53683898 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…
|
| ZINC8586019 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…
|
| ZINC8586020 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…
|
| ZINC8586021 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC8586022 ZINC | 0.651 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…
|
| ZINC169620381 ZINC | 0.649 | 261.3 Da LogP 2.36 TPSA 52.3 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1cccs1)C(=O)OCc1ccccc1
|
| ZINC106686432 ZINC | 0.641 | 428.2 Da LogP -2.03 TPSA 226.5 | 2 viol. | ✓ Clean |
O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP…
|
| ZINC12958393 ZINC | 0.641 | 428.2 Da LogP -2.03 TPSA 226.5 | 2 viol. | ✓ Clean |
O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)O…
|
| ZINC35024781 ZINC | 0.641 | 428.2 Da LogP -2.03 TPSA 226.5 | 2 viol. | ✓ Clean |
O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…
|
| ZINC35024785 ZINC | 0.641 | 428.2 Da LogP -2.03 TPSA 226.5 | 2 viol. | ✓ Clean |
O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…
|
| ZINC35024786 ZINC | 0.641 | 428.2 Da LogP -2.03 TPSA 226.5 | 2 viol. | ✓ Clean |
O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)…
|
| ZINC4261903 ZINC | 0.641 | 428.2 Da LogP -2.03 TPSA 226.5 | 2 viol. | ✓ Clean |
O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…
|
| ZINC80601236 ZINC | 0.641 | 428.2 Da LogP -2.03 TPSA 226.5 | 2 viol. | ✓ Clean |
O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…
|
| ZINC95921560 ZINC | 0.641 | 428.2 Da LogP -2.03 TPSA 226.5 | 2 viol. | ✓ Clean |
O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…
|
| ZINC1671214 ZINC | 0.636 | 238.3 Da LogP 3.22 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@@H](Cc1cccs1)c1cccs1
|
| ZINC2042523 ZINC | 0.636 | 238.3 Da LogP 3.22 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H](Cc1cccs1)c1cccs1
|
| ZINC17375772 ZINC | 0.621 | 459.3 Da LogP -1.46 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1nc(S)c2ncn([C@@H]3O[C@@H](CO[P@](=O)(O)OP(=O…
|
| ZINC8618621 ZINC | 0.621 | 459.3 Da LogP -1.46 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1nc(S)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC8618622 ZINC | 0.621 | 459.3 Da LogP -1.46 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1nc(S)c2ncn([C@@H]3O[C@@H](CO[P@@](=O)(O)OP(=…
|
| ZINC8618623 ZINC | 0.621 | 459.3 Da LogP -1.46 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1nc(S)c2ncn([C@H]3O[C@@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC37437 ZINC | 0.618 | 232.3 Da LogP 3.16 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H](Cc1cccs1)c1ccccc1
|
| ZINC37438 ZINC | 0.618 | 232.3 Da LogP 3.16 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@@H](Cc1cccs1)c1ccccc1
|
| ZINC34619851 ZINC | 0.611 | 214.2 Da LogP 1.16 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@@H](Cc1cccs1)C(=O)O
|
| ZINC34619853 ZINC | 0.611 | 214.2 Da LogP 1.16 TPSA 63.6 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@H](Cc1cccs1)C(=O)O
|
| ZINC13521831 ZINC | 0.600 | 492.2 Da LogP -1.21 TPSA 253.1 | 2 viol. | ✓ Clean |
O=P(O)(O)O[P@](=O)(O)O[P@](=O)(O)OC[C@H]1O[C@@H…
|
| ZINC4419531 ZINC | 0.600 | 214.2 Da LogP 1.47 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)C[C@H](Cc1cccs1)C(=O)O
|
| ZINC4419532 ZINC | 0.600 | 214.2 Da LogP 1.47 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)C[C@@H](Cc1cccs1)C(=O)O
|
| ZINC33902382 ZINC | 0.597 | 461.6 Da LogP -1.09 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1nc(Cl)nc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…
|
| ZINC33902769 ZINC | 0.597 | 445.2 Da LogP -1.61 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP…
|
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.
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.