Protein target profile

HT085_RS00315

formate--tetrahydrofolate ligase

Genome: NZ_AP023069.1 Gene: N776_09010 TUM19854C_00530 fhs NGK_0086 3D evidence: AlphaFold DB model UniProt B4RP08 UniProt A0AA44U8Q2
Length 558
Direct ligand evidence 0 61 total records
Functional annotation 1 EC 3 GO
Target summary

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.

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
Hit
Gut microbiome off-target
Hit

Essentiality

Essential (DEG)
Y

Localization

Localization
Cytoplasmic

Binding-site evidence

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 Low
Structure
Pocket

Sequence

Primary amino-acid sequence viewer.

MSFKTDAETAQSSTMRPIGEIAAKLGLNVDNIEPYGHYKAKINPAEAFKLPQKQGRLILVTAINPTPAGEGKTTVTIGLADALRHIGKDSVIALREPSLGPVFGVKGGAAGGGYAQVLPMEDINLHFTGDFHAIGAANNLLAAMLDNHIYQGNELNIDPKRVLWRRVVDMNDRQLRNIIDGMGKPVDGVMRPDGFDITVASEVMAVFCLAKDISDLKERFGNILVAYAKDGSPVYAKDLKAHGAMAALLKDAIKPNLVQTIEGTPAFVHGGPFANIAHGCNSVTATRLAKHLADYAVTEAGFGADLGAEKFCDIKCRLAGLKPDAAVVVATVRALKYNGGVERANLGEENLEALAKGLPNLLKHISNLKNVFGLPVVVALNRFVSDSDAELAMIEKACAEHGVEVSLTEVWGKGGAGGADLARKVVNAIDNQPNNFGFAYDVELGIKDKIRAIAQKVYGAEDVDFSAEASAEIASLEKLGLDKMPICMAKTQYSLSDNAKLLGCPEGFRITVRGITVSAGAGFIVALCGNMMKMPGLPKVPAAEKIDVDEHGVIHGLF

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

3
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0004329 Catalysis of the reaction: ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.
  • GO:0035999 The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesize other tetrahydrofolate molecules.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

21 records
Show feature table
Start End DB Term Name
5 427 Gene3D G3DSA:3.40.50.300 -
5 427 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
445 534 Gene3D G3DSA:3.10.410.10 Formyltetrahydrofolate synthetase, domain 3
130 248 Gene3D G3DSA:3.30.1510.10 -
329 340 ProSitePatterns PS00722 Formate--tetrahydrofolate ligase signature 2.
329 340 InterPro IPR020628 Formate-tetrahydrofolate ligase, FTHFS, conserved site
1 509 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
445 534 FunFam G3DSA:3.10.410.10:FF:000001 Putative formate--tetrahydrofolate ligase
4 558 Pfam PF01268 Formate--tetrahydrofolate ligase
4 558 InterPro IPR000559 Formate-tetrahydrofolate ligase, FTHFS
130 248 FunFam G3DSA:3.30.1510.10:FF:000001 Formate--tetrahydrofolate ligase
3 558 Hamap MF_01543 Formate--tetrahydrofolate ligase [fhs].
3 558 InterPro IPR000559 Formate-tetrahydrofolate ligase, FTHFS
104 114 ProSitePatterns PS00721 Formate--tetrahydrofolate ligase signature 1.
104 114 InterPro IPR020628 Formate-tetrahydrofolate ligase, FTHFS, conserved site
6 556 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
6 556 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
530 558 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
18 557 CDD cd00477 FTHFS
18 557 InterPro IPR000559 Formate-tetrahydrofolate ligase, FTHFS
510 529 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.

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 #11
0.438
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Surrounding area
Site 2 FPocket #4
0.343
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Surrounding area
Site 3 FPocket #2
0.318
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Surrounding area
Site 4 FPocket #10
0.296
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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
0.843
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Surrounding area
Site 2 P2Rank #2
0.309
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Surrounding area
Site 3 P2Rank #3
0.025
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Surrounding area
Site 4 P2Rank #4
0.014
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Surrounding area
All structural evidence 0 experimental · 1 predicted

Structural evidence

0 + 1

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 HT085_RS00315
AlphaFold DB full sequence Viewing

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.

61 records
Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records
Transferred evidence 11 records from similar proteins
Structural ligands 9 0 loaded crystals
Measured bioactivity 2 direct and transferred ChEMBL records
Proposed compounds 50 similarity-based ZINC candidates
Best available ligand signal
21V PDB via homolog 443.5 Da · LogP 0.62 · TPSA 187.5 Open detail RCSB PDB
FLC PDB via homolog Detail RCSB PDB
FOL PDB via homolog Detail RCSB PDB
L37 PDB via homolog Detail RCSB PDB
TAR 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
21V RCSB PDB P11586 443.5 Da LogP 0.62 TPSA 187.5 1 viol. ✓ Clean c1cc(ccc1CC[C@H]2CC3=C(NC2)NC(=NC3=O)N)C(=O)N[C…
FLC RCSB PDB B7L0A5 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
FOL RCSB PDB Q2RM91 441.4 Da LogP -0.04 TPSA 213.3 1 viol. ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NCc2cnc3c…
L37 RCSB PDB P11586 433.4 Da LogP 0.04 TPSA 242.9 1 viol. ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)Nc2…
TAR RCSB PDB K7SWE7 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@H]([C@@H](C(=O)O)O)(C(=O)O)O
TLA RCSB PDB B7L0A5 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=O)O)O
TOE RCSB PDB Q2RM91 164.2 Da LogP -0.34 TPSA 47.9 ✓ Ro5 ✓ Clean COCCOCCOCCO
XPO RCSB PDB Q2RM91 126.0 Da LogP -0.75 TPSA 83.8 ✓ Ro5 ✓ Clean C(=O)OP(=O)(O)O
ZD9 RCSB PDB Q2RM91 241.3 Da LogP 1.61 TPSA 57.8 ✓ Ro5 ✓ Clean CC#CNCc1cc2c(cc1C)N=C(NC2=O)C

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.