Protein target profile

KP13_01359

50S ribosomal protein L7/L12

Genome: KpKP13 Gene: rplL AHE46940.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GH99
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Length 121
Pocket druggability 0.017
Functional annotation 0 EC 5 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Structure available AlphaFold DB model + ColabFold model

Risks to review

Human similarity Top human hit identity: 38.667%. Microbiome similarity 2850 of 4744 screened genomes (60.1%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.02.

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein. No ligand evidence No experimental PDB ligands, measured ChEMBL bioactivity, or proposed ZINC compound records are 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
Human identity (%)
38.667 Lower values reduce human off-target concern.
Human E-value
7.16e-06
Gut microbiome similarity
60.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
Y
DEG identity (%)
98.347 Higher values support similarity to known essential genes.
DEG E-value
1.83e-75 Smaller values mean stronger essential-gene similarity.

Localization

Localization
Unknown

Structure confidence

ColabFold pLDDT
75.9 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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 0.017
Structure A0A0H3GH99
Pocket Pocket 4
P2Rank
Structure A0A0H3GH99
Pocket No pockets
ColabFold model
FPocket 0.506 · Pocket 3
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 2850 / 4744 genomes with a hit
Prevalence 60.1%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GH99

Sequence

Primary amino-acid sequence viewer.

MSITKDQIIEAVSAMSVMDVVELISAMEEKFGVSAAAAVAVAAGPVEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGISKDDAEALKKSLEEAGAEVEVK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
  • GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
  • GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
  • GO:0022625 The large subunit of a ribosome located in the cytosol.
  • GO:0003729 Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records
Show feature table
Start End DB Term Name
55 121 Pfam PF00542 Ribosomal protein L7/L12 C-terminal domain
55 121 InterPro IPR013823 Ribosomal protein L7/L12, C-terminal
101 121 Coils Coil Coil
6 120 PANTHER PTHR45987 39S RIBOSOMAL PROTEIN L12
6 120 InterPro IPR000206 Ribosomal protein L7/L12
3 120 CDD cd00387 Ribosomal_L7_L12
3 120 InterPro IPR000206 Ribosomal protein L7/L12
50 121 SUPERFAMILY SSF54736 ClpS-like
50 121 InterPro IPR014719 Ribosomal protein L7/L12, C-terminal/adaptor protein ClpS-like
3 57 SUPERFAMILY SSF48300 Ribosomal protein L7/12, oligomerisation (N-terminal) domain
3 57 InterPro IPR036235 Ribosomal protein L7/L12, oligomerisation domain superfamily
1 121 NCBIfam TIGR00855 50S ribosomal protein L7/L12
1 121 InterPro IPR000206 Ribosomal protein L7/L12
51 121 FunFam G3DSA:3.30.1390.10:FF:000001 50S ribosomal protein L7/L12
2 50 Gene3D G3DSA:1.20.5.710 Single helix bin
2 50 InterPro IPR036235 Ribosomal protein L7/L12, oligomerisation domain superfamily
2 50 FunFam G3DSA:1.20.5.710:FF:000001 50S ribosomal protein L7/L12
4 49 Pfam PF16320 Ribosomal protein L7/L12 dimerisation domain
4 49 InterPro IPR008932 Ribosomal protein L7/L12, oligomerisation
51 121 Gene3D G3DSA:3.30.1390.10 -
51 121 InterPro IPR014719 Ribosomal protein L7/L12, C-terminal/adaptor protein ClpS-like
2 121 Hamap MF_00368 50S ribosomal protein L7/L12 [rplL].
2 121 InterPro IPR000206 Ribosomal protein L7/L12

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
All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

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 AF_A0A0H3GH99
AlphaFold DB — — full sequence — Viewing
ColabFold KP13_01359
ColabFold — — full sequence — Loaded