Protein target profile

HT085_RS00225

acetyl-CoA carboxylase biotin carboxylase subunit

Genome: NZ_AP023069.1 Gene: E8M63_06595 accC ESCNG_30007 TUM19854C_00360 3D evidence: AlphaFold DB model UniProt A0AAX2TQ28
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Length 453
Direct ligand evidence 0 95 total records
Functional annotation 1 EC 4 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.

Main supporting evidence

Structure available AlphaFold DB model Ligand evidence via structure/bioactivity 30 structural and 15 bioactivity records.

Risks to review

Human similarity A significant human homolog was found.

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein. No FPocket pocket score No selected computational pocket-druggability value is available.
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 Medium
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MLKKVLIANRGEIALRVLRACREMGIATVAVHSEADKGSLHVKLADESVCIGPAASAQSYLNIPAIIAAAEVTCADAVHPGYGFLAENADFAEQVEQSGFTFIGPKPDTIRLMGDKVSAKHAMIAAGVPCVPGSDGALPDDDAEILKIADKVGYPVIIKASGGGGGRGMRVVEKKEDLLQSVEMTKAEAGAAFGNPMVYMERYLQRPRHVEIQVLADEHGNAVYLAERDCSLQRRHQKVIEEAPAPFIDEEARKKIGKACTDACKRIGYRGAGTFEFLYEDGEFFFIEMNTRVQVEHPVTELITGVDIVQEQLRIASGLPLQYKQKDIKIEGHAFECRINAEDPYNFIPSPGPIESCHLPGGFGIRVDSHIYQGYRIPPYYDSLIGKICVHGKTREQAMAKMRVALAELAVTGIKTNTPLHRDLFADAGFQEGGVSIHYLEHWLEARKTKQDK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

4
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0046872 Binding to a metal ion.
  • GO:0004075 Catalysis of the reaction: ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
  • GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

29 records
Show feature table
Start End DB Term Name
1 131 FunFam G3DSA:3.40.50.20:FF:000010 Propionyl-CoA carboxylase subunit alpha
1 445 ProSiteProfiles PS50979 Biotin carboxylation domain profile.
1 445 InterPro IPR011764 Biotin carboxylation domain
204 443 Gene3D G3DSA:3.30.470.20 -
1 445 NCBIfam TIGR00514 acetyl-CoA carboxylase biotin carboxylase subunit
1 445 InterPro IPR004549 Acetyl-CoA carboxylase, biotin carboxylase
331 444 SUPERFAMILY SSF51246 Rudiment single hybrid motif
331 444 InterPro IPR011054 Rudiment single hybrid motif
154 168 ProSitePatterns PS00866 Carbamoyl-phosphate synthase subdomain signature 1.
154 168 InterPro IPR005479 Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
1 110 Pfam PF00289 Biotin carboxylase, N-terminal domain
1 110 InterPro IPR005481 Biotin carboxylase-like, N-terminal domain
1 131 Gene3D G3DSA:3.40.50.20 -
120 317 ProSiteProfiles PS50975 ATP-grasp fold profile.
120 317 InterPro IPR011761 ATP-grasp fold
336 441 Pfam PF02785 Biotin carboxylase C-terminal domain
336 441 InterPro IPR005482 Biotin carboxylase, C-terminal
1 113 SUPERFAMILY SSF52440 PreATP-grasp domain
1 113 InterPro IPR016185 Pre-ATP-grasp domain superfamily
286 293 ProSitePatterns PS00867 Carbamoyl-phosphate synthase subdomain signature 2.
286 293 InterPro IPR005479 Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
132 203 Gene3D G3DSA:3.30.1490.20 -
132 203 InterPro IPR013815 ATP-grasp fold, subdomain 1
336 441 SMART SM00878 Biotin_carb_C_2
83 347 SUPERFAMILY SSF56059 Glutathione synthetase ATP-binding domain-like
3 447 PANTHER PTHR48095 PYRUVATE CARBOXYLASE SUBUNIT A
115 322 Pfam PF02786 Carbamoyl-phosphate synthase L chain, ATP binding domain
115 322 InterPro IPR005479 Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
132 203 FunFam G3DSA:3.30.1490.20:FF:000003 acetyl-CoA carboxylase isoform X1

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 #1
0.622
Likely same site as P2Rank 1 4.5 Å 43 shared residues 91% of smaller site
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Surrounding area
Site 2 FPocket #2
0.21
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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
0.906
Likely same site as FPocket 1 4.5 Å 43 shared residues 91% of smaller site
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Surrounding area
Site 2 P2Rank #2
0.042
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Surrounding area
Site 3 P2Rank #3
0.011
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Surrounding area
Site 4 P2Rank #4
0.005
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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_RS00225
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.

95 records
Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records
Transferred evidence 45 records from similar proteins
Structural ligands 30 0 loaded crystals
Measured bioactivity 15 direct and transferred ChEMBL records
Proposed compounds 50 similarity-based ZINC candidates
Best available ligand signal
3PY PDB via homolog 104.1 Da · LogP -1.37 · TPSA 74.6 Open detail RCSB PDB
ACP PDB via homolog Detail RCSB PDB
AGS PDB via homolog Detail RCSB PDB
ANP PDB via homolog Detail RCSB PDB
BPV 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
3PY RCSB PDB
4MFE
Q2K340 104.1 Da LogP -1.37 TPSA 74.6 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)O
ACP RCSB PDB
4MV8
P43873 505.2 Da LogP -1.52 TPSA 269.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
AGS RCSB PDB
2QF7
Q2K340 523.2 Da LogP -1.51 TPSA 262.1 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
ANP RCSB PDB
3OUU
Q0P8W7 506.2 Da LogP -2.06 TPSA 281.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
BPV RCSB PDB
4MIM
Q2K340 167.0 Da LogP 0.03 TPSA 54.4 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)Br
BTI RCSB PDB
3TW6
Q2K340 228.3 Da LogP 0.91 TPSA 58.2 ✓ Ro5 ✓ Clean C1[C@H]2[C@@H]([C@@H](S1)CCCCC=O)NC(=O)N2
BYT RCSB PDB
4M6V
Q2K340 372.5 Da LogP 0.41 TPSA 133.6 ✓ Ro5 ✓ Clean C1[C@H]2[C@@H]([C@@H](S1)CCCCC(=O)NCCCC[C@@H](C…
CAC RCSB PDB
3OUU
Q0P8W7 137.0 Da LogP -0.52 TPSA 40.1 ✓ Ro5 ✓ Clean C[As](=O)(C)[O-]
JZK RCSB PDB
3JZF
P24182 396.9 Da LogP 4.98 TPSA 72.9 ✓ Ro5 ✓ Clean c1ccc(c(c1)CNc2nc3cc(ccc3n2CC4CCCCC4)C(=O)N)Cl
JZL RCSB PDB
3JZI
P24182 442.0 Da LogP 3.92 TPSA 119.2 ✓ Ro5 ✓ Clean c1ccc(c(c1)CNc2nc3cc(cc(c3n2C[C@@H]4CCCCC[C@@H]…
L21 RCSB PDB
2W6Z
P24182 203.2 Da LogP 1.33 TPSA 69.6 ✓ Ro5 ✓ Clean CC(=CCn1cnc(c-2ncnc12)N)C
L22 RCSB PDB
2W70
P24182 193.2 Da LogP 0.76 TPSA 90.7 ✓ Ro5 ✓ Clean c1cnc(nc1c2csc(n2)N)N
L23 RCSB PDB
2W71
P24182 334.2 Da LogP 3.59 TPSA 69.6 ✓ Ro5 ✓ Clean Cc1nc(cn1Cc2c(cccc2Cl)Cl)c3ccnc(n3)N
MLT RCSB PDB
3OUZ
Q0P8W7 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)O)C(=O)O
MQM RCSB PDB
6OI9
P24182 389.3 Da LogP 3.37 TPSA 94.0 ✓ Ro5 ✓ Clean c1cc(c(c(c1)Cl)c2cc3cnc(nc3nc2N4CC[C@H](C4)CN)N…
MQV RCSB PDB
6OI8
P43873 429.9 Da LogP 3.38 TPSA 106.8 ✓ Ro5 ✓ Clean c1cc(c(c(c1)Cl)c2cc3cnc(nc3nc2N4C[C@@H]5[C@H](C…
MV4 RCSB PDB
6OJH
P43873 356.4 Da LogP 2.96 TPSA 94.0 ✓ Ro5 ✓ Clean c1ccc2c(c1)cccc2c3cc4cnc(nc4nc3N5CC[C@H](C5)N)N
OA1 RCSB PDB
2W6M
P24182 267.1 Da LogP 2.25 TPSA 69.1 ✓ Ro5 ✓ Clean c1cc(cc(c1)Br)C(=O)c2cnc(o2)N
OA2 RCSB PDB
2W6N
P24182 307.4 Da LogP 3.10 TPSA 72.4 ✓ Ro5 ✓ Clean c1ccc(cc1)CN(Cc2ccccc2)C(=O)c3cnc(o3)N
OA3 RCSB PDB
2W6O
P24182 191.2 Da LogP 1.21 TPSA 68.9 ✓ Ro5 ✓ Clean CC1(Cc2c(c(ncn2)N)C(=O)C1)C
OA4 RCSB PDB
2W6P
P24182 250.3 Da LogP 2.77 TPSA 77.8 ✓ Ro5 ✓ Clean Cc1c(ccc2c1c(nc(n2)N)N)c3ccccc3
OA5 RCSB PDB
2W6Q
P24182 247.3 Da LogP 0.49 TPSA 109.2 ✓ Ro5 ✓ Clean c1ccc(cc1)OCCOc2nc(nc(n2)N)N
OXL RCSB PDB
4MFD
Q2K340 88.0 Da LogP -3.51 TPSA 80.3 ✓ Ro5 ✓ Clean C(=O)(C(=O)[O-])[O-]
PAE RCSB PDB
3TW6
Q2K340 140.0 Da LogP -0.75 TPSA 94.8 ✓ Ro5 ✓ Clean C(C(=O)O)P(=O)(O)O
PCT RCSB PDB
4MV6
P43873 139.0 Da LogP -1.35 TPSA 100.6 ✓ Ro5 ✓ Clean C(C(=O)N)P(=O)(O)O
PPF RCSB PDB
4MV7
P43873 126.0 Da LogP -0.16 TPSA 94.8 ✓ Ro5 ✓ Clean C(=O)(O)P(=O)(O)O
PYR RCSB PDB
4JX5
Q2K340 88.1 Da LogP -0.34 TPSA 54.4 ✓ Ro5 ✓ Clean CC(=O)C(=O)O
SRT RCSB PDB
3OUZ
Q0P8W7 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
3OUZ
Q0P8W7 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=O)O)O
Y7Y RCSB PDB
4RZQ
P43873 316.4 Da LogP 1.36 TPSA 84.9 ✓ Ro5 ✓ Clean COC(=O)CCCC[C@H]1[C@@H]2[C@H](CS1)N(C(=O)N2)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.