Overview
Basic information about this protein and its source genome.
- Accession
- KP13_02520
- Gene
- AHE42984.1 nlpD
- Status
- annotated
- Amino acids
- 378
- 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
- OuterMembrane
- ColabFold pLDDT
- 68.26
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.
Gene Ontology (GO)
5- GO:0032153 The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
- GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.
- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
- GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
- GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 12 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 167 | 187 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 213 | 376 | FunFam | G3DSA:2.70.70.10:FF:000004 | NlpD family lipoprotein |
| 108 | 166 | FunFam | G3DSA:3.10.350.10:FF:000008 | Murein hydrolase activator NlpD |
| 114 | 157 | Gene3D | G3DSA:3.10.350.10 | LysM domain |
| 114 | 157 | InterPro | IPR036779 | LysM domain superfamily |
| 115 | 158 | CDD | cd00118 | LysM |
| 115 | 158 | InterPro | IPR018392 | LysM domain |
| 116 | 158 | Pfam | PF01476 | LysM domain |
| 116 | 158 | InterPro | IPR018392 | LysM domain |
| 39 | 378 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 278 | 371 | Pfam | PF01551 | Peptidase family M23 |
| 278 | 371 | InterPro | IPR016047 | Peptidase M23 |
| 115 | 375 | SUPERFAMILY | SSF51261 | Duplicated hybrid motif |
| 115 | 375 | InterPro | IPR011055 | Duplicated hybrid motif |
| 1 | 29 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 115 | 159 | SMART | SM00257 | LysM_2 |
| 115 | 159 | InterPro | IPR018392 | LysM domain |
| 13 | 26 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 38 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 35 | 86 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 1 | 26 | ProSiteProfiles | PS51257 | Prokaryotic membrane lipoprotein lipid attachment site profile. |
| 278 | 362 | CDD | cd12797 | M23_peptidase |
| 107 | 375 | PANTHER | PTHR21666 | PEPTIDASE-RELATED |
| 219 | 376 | Gene3D | G3DSA:2.70.70.10 | Glucose Permease (Domain IIA) |
| 219 | 376 | InterPro | IPR011055 | Duplicated hybrid motif |
| 1 | 25 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 114 | 158 | ProSiteProfiles | PS51782 | LysM domain profile. |
| 114 | 158 | InterPro | IPR018392 | LysM domain |
| 27 | 38 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 63 | 86 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 35 | 55 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 1 | 24 | SignalP_GRAM_NEGATIVE | SignalP-noTM | SignalP-noTM |
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_A0A0H3GWT3
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_02520
|
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 | 5.13 | 0.235 | ||||||
| 2 | 2.89 | 0.092 | ||||||
| 3 | 1.64 | 0.027 |
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 16 | 0.749 |
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 | 7.2 | 0.375 | ||||||
| 2 | 5.38 | 0.255 | ||||||
| 3 | 2.02 | 0.044 | ||||||
| 4 | 1.5 | 0.021 |
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 |
|---|---|---|---|---|---|---|
| 4SQ | O33599 | 281.2 Da LogP -2.12 TPSA 158.8 | ✓ Ro5 | ✓ Clean |
C(CP(=O)(CNC(=O)CN)O)C(=O)NCC(=O)O
|
|
| CAC | O33599 | 137.0 Da LogP -0.52 TPSA 40.1 | ✓ Ro5 | ✓ Clean |
C[As](=O)(C)[O-]
|
|
| TLA | O33599 | 150.1 Da LogP -2.12 TPSA 115.1 | ✓ Ro5 | ✓ Clean |
[C@@H]([C@H](C(=O)O)O)(C(=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 |
|---|---|---|---|---|---|
| ZINC12359024 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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
|
| ZINC1560405156 | 0.588 | 208.1 Da LogP -1.79 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC1560405157 | 0.588 | 208.1 Da LogP -1.79 TPSA 155.5 | 1 viol. | ✓ Clean |
O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O
|
| ZINC2561009 | 0.571 | 203.2 Da LogP -2.35 TPSA 121.5 | ✓ Ro5 | ✓ Clean |
NCC(=O)NCCC(=O)NCC(=O)O
|
| ZINC1569725 | 0.545 | 246.2 Da LogP -3.62 TPSA 150.6 | ✓ Ro5 | ✓ Clean |
NCC(=O)NCC(=O)NCC(=O)NCC(=O)O
|
| ZINC4545903 | 0.545 | 360.3 Da LogP -5.39 TPSA 208.8 | 1 viol. | ✓ Clean |
NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)O
|
| ZINC4545906 | 0.545 | 303.3 Da LogP -4.51 TPSA 179.7 | 1 viol. | ✓ Clean |
NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)O
|
| ZINC1529331 | 0.500 | 206.1 Da LogP -2.21 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)C(=O)[C@H](C(=O)O)[C@@H](O)C(=O)O
|
| ZINC1529332 | 0.500 | 206.1 Da LogP -2.21 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)C(=O)[C@H](C(=O)O)[C@H](O)C(=O)O
|
| ZINC1529333 | 0.500 | 206.1 Da LogP -2.21 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)C(=O)[C@@H](C(=O)O)[C@@H](O)C(=O)O
|
| ZINC1529334 | 0.500 | 206.1 Da LogP -2.21 TPSA 149.2 | ✓ Ro5 | ✓ Clean |
O=C(O)C(=O)[C@@H](C(=O)O)[C@H](O)C(=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.