Overview
Basic information about this protein and its source genome.
- Accession
- KP13_00965
- Gene
- AHE43505.1
- Status
- annotated
- Amino acids
- 273
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- DEG identity (%)
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 92.58
Selected Druggability evidence
AlphaFold / UniProt modelSelected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
5- GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
- GO:0016832 Catalysis of the cleavage of a C-C bond in a molecule containing a hydroxyl group and a carbonyl group to form two smaller molecules, each being an aldehyde or a ketone.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0106099 Catalysis of the reaction 2-dehydro-3-deoxy-L-rhamnonate = pyruvate + (S)-lactaldehyde.
- GO:0000287 Binding to a magnesium (Mg) ion.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 25 | 251 | Pfam | PF03328 | HpcH/HpaI aldolase/citrate lyase family |
| 25 | 251 | InterPro | IPR005000 | HpcH/HpaI aldolase/citrate lyase domain |
| 10 | 263 | SUPERFAMILY | SSF51621 | Phosphoenolpyruvate/pyruvate domain |
| 10 | 263 | InterPro | IPR015813 | Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily |
| 7 | 273 | Gene3D | G3DSA:3.20.20.60 | - |
| 7 | 273 | InterPro | IPR040442 | Pyruvate kinase-like domain superfamily |
| 7 | 273 | Hamap | MF_01290 | 2-keto-3-deoxy-L-rhamnonate aldolase [rhmA]. |
| 7 | 273 | InterPro | IPR023593 | 2-keto-3-deoxy-L-rhamnonate aldolase |
| 12 | 271 | PANTHER | PTHR30502 | 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE |
| 6 | 262 | FunFam | G3DSA:3.20.20.60:FF:000004 | 5-keto-4-deoxy-D-glucarate aldolase |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3H0Z2
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_00965
|
ColabFold | — | — | full sequence | — | Loaded |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 10.18 | 0.548 | ||||||
| 2 | 2.15 | 0.05 | ||||||
| 3 | 1.15 | 0.009 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 3.87 | 0.151 | ||||||
| 2 | 2.14 | 0.05 |
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.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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 |
|---|---|---|---|---|---|---|
| 2KT | B1IS70 | 102.1 Da LogP 0.05 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCC(=O)C(=O)O
|
|
| 3GR | B1IS70 | 90.1 Da LogP -1.46 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
C([C@H](C=O)O)O
|
|
| 3PY | A0A9J9HGY6 | 104.1 Da LogP -1.37 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
C(C(=O)C(=O)O)O
|
|
| E8U | B1IS70 | 190.2 Da LogP -0.74 TPSA 111.9 | ✓ Ro5 | ✓ Clean |
C(CC(=O)O)[C@H](CC(=O)C(=O)O)O
|
|
| OAA | A0A0H3K9Z0 | 131.1 Da LogP -2.22 TPSA 94.5 | ✓ Ro5 | ✓ Clean |
C(C(=O)C(=O)O)C(=O)[O-]
|
|
| PYR | B1IS70 | 88.1 Da LogP -0.34 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CC(=O)C(=O)O
|
|
| SSN | B1IS70 | 102.1 Da LogP 0.05 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
C(CC(=O)O)C=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 |
|---|---|---|---|---|---|
| ZINC114311466 | 0.619 | 256.4 Da LogP 4.34 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=CCCCCCCCCCCCCCC(=O)O
|
| ZINC117784029 | 0.619 | 242.4 Da LogP 3.95 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=CCCCCCCCCCCCCC(=O)O
|
| ZINC13512355 | 0.619 | 200.3 Da LogP 2.78 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=CCCCCCCCCCC(=O)O
|
| ZINC13546209 | 0.619 | 270.4 Da LogP 4.73 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=CCCCCCCCCCCCCCCC(=O)O
|
| ZINC5178596 | 0.619 | 214.3 Da LogP 3.17 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=CCCCCCCCCCCC(=O)O
|
| ZINC33822324 | 0.609 | 228.3 Da LogP 2.35 TPSA 71.4 | ✓ Ro5 | ✓ Clean |
O=CCCC(=O)CCCCCCCC(=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.