Amino acids
474
Annotations
6
Features
52
PDB binders
3
Druggability
0.859
Overview
Basic information about this protein and its source genome.
- Accession
- PA0766
- Gene
- mucD_1 PAERUG_P19_London_7_VIM_2_05_10_02248 PA0766 mucD CAZ10_12495
- Status
- annotated
- Amino acids
- 474
- Structure source
- AlphaFold
EC
GO
GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
GO:0005515 Binding to a protein.
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 43.558
- Human E-value
- 1.7799999999999994e-24
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- Localization
- Periplasmic
Selected Druggability evidence
Selected 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.
FPocket
0.859
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
5 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
5- GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
- GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
- GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
- GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
- GO:0005515 Binding to a protein.
Sequence Features
Domain/signature hits from InterPro and related databases.
52 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 6 | 279 | SUPERFAMILY | SSF50494 | Trypsin-like serine proteases |
| 6 | 279 | InterPro | IPR009003 | Peptidase S1, PA clan |
| 28 | 263 | FunFam | G3DSA:2.40.10.120:FF:000007 | Periplasmic serine endoprotease DegP-like |
| 26 | 474 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 1 | 8 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 21 | 25 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 1 | 25 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 27 | 263 | Gene3D | G3DSA:2.40.10.120 | - |
| 270 | 359 | CDD | cd00987 | PDZ_serine_protease |
| 28 | 470 | NCBIfam | TIGR02037 | Do family serine endopeptidase |
| 28 | 470 | InterPro | IPR011782 | Peptidase S1C, Do |
| 239 | 376 | Pfam | PF02163 | Peptidase family M50 |
| 239 | 376 | InterPro | IPR008915 | Peptidase M50 |
| 23 | 362 | PANTHER | PTHR22939 | SERINE PROTEASE FAMILY S1C HTRA-RELATED |
| 1 | 25 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 261 | 352 | ProSiteProfiles | PS50106 | PDZ domain profile. |
| 261 | 352 | InterPro | IPR001478 | PDZ domain |
| 268 | 369 | FunFam | G3DSA:2.30.42.10:FF:000037 | Periplasmic serine endoprotease DegP-like |
| 9 | 20 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 272 | 359 | Pfam | PF13180 | PDZ domain |
| 272 | 359 | InterPro | IPR001478 | PDZ domain |
| 386 | 466 | Pfam | PF13180 | PDZ domain |
| 386 | 466 | InterPro | IPR001478 | PDZ domain |
| 128 | 148 | PRINTS | PR00834 | HtrA/DegQ protease family signature |
| 128 | 148 | InterPro | IPR001940 | Peptidase S1C |
| 310 | 322 | PRINTS | PR00834 | HtrA/DegQ protease family signature |
| 310 | 322 | InterPro | IPR001940 | Peptidase S1C |
| 107 | 119 | PRINTS | PR00834 | HtrA/DegQ protease family signature |
| 107 | 119 | InterPro | IPR001940 | Peptidase S1C |
| 168 | 192 | PRINTS | PR00834 | HtrA/DegQ protease family signature |
| 168 | 192 | InterPro | IPR001940 | Peptidase S1C |
| 202 | 219 | PRINTS | PR00834 | HtrA/DegQ protease family signature |
| 202 | 219 | InterPro | IPR001940 | Peptidase S1C |
| 224 | 241 | PRINTS | PR00834 | HtrA/DegQ protease family signature |
| 224 | 241 | InterPro | IPR001940 | Peptidase S1C |
| 1 | 25 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 382 | 463 | ProSiteProfiles | PS50106 | PDZ domain profile. |
| 382 | 463 | InterPro | IPR001478 | PDZ domain |
| 98 | 231 | Pfam | PF13365 | Trypsin-like peptidase domain |
| 385 | 472 | SUPERFAMILY | SSF50156 | PDZ domain-like |
| 385 | 472 | InterPro | IPR036034 | PDZ superfamily |
| 384 | 463 | SMART | SM00228 | pdz_new |
| 384 | 463 | InterPro | IPR001478 | PDZ domain |
| 270 | 352 | SMART | SM00228 | pdz_new |
| 270 | 352 | InterPro | IPR001478 | PDZ domain |
| 268 | 369 | Gene3D | G3DSA:2.30.42.10 | - |
| 268 | 369 | InterPro | IPR036034 | PDZ superfamily |
| 385 | 470 | CDD | cd00987 | PDZ_serine_protease |
| 252 | 358 | SUPERFAMILY | SSF50156 | PDZ domain-like |
| 252 | 358 | InterPro | IPR036034 | PDZ superfamily |
| 381 | 474 | Gene3D | G3DSA:2.30.42.10 | - |
| 381 | 474 | InterPro | IPR036034 | PDZ superfamily |
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...
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Medium
Low
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA0766
|
AlphaFold | — | — | full sequence | — | Viewing |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.248 | ||||||
| 6 | 0.215 |
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.
53 records
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 |
|---|---|---|---|---|---|---|
| CXS | A0A5P8YL96 | 221.3 Da LogP 1.19 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
C1CCC(CC1)NCCCS(=O)(=O)O
|
|
| DFP | P0C0V0 | 166.2 Da LogP 2.23 TPSA 35.5 | ✓ Ro5 | ✓ Clean |
CC(C)OP(=O)OC(C)C
|
|
| PMS | O06291 | 172.2 Da LogP 1.07 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
c1ccc(cc1)CS(=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 |
|---|---|---|---|---|---|
| ZINC2004372 | 1.000 | 221.3 Da LogP 1.19 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCNC1CCCCC1
|
| ZINC38364153 | 0.926 | 235.3 Da LogP 1.58 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCCNC1CCCCC1
|
| ZINC1710230 | 0.786 | 207.3 Da LogP 0.80 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCNC1CCCCC1
|
| ZINC1764974 | 0.750 | 266.3 Da LogP 0.46 TPSA 108.7 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)Cc1ccc(CS(=O)(=O)O)cc1
|
| ZINC389634 | 0.714 | 246.3 Da LogP 2.80 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)Cc1ccccc1
|
| ZINC5188799 | 0.630 | 280.5 Da LogP 4.39 TPSA 24.1 | ✓ Ro5 | ✓ Clean |
C(CCCNC1CCCCC1)CCNC1CCCCC1
|
| ZINC34080186 | 0.609 | 266.3 Da LogP 0.46 TPSA 108.7 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)Cc1ccccc1CS(=O)(=O)O
|
| ZINC32210235 | 0.600 | 251.1 Da LogP 1.84 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)Cc1ccc(Br)cc1
|
| ZINC1679108 | 0.583 | 324.4 Da LogP 2.17 TPSA 68.3 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)CS(=O)(=O)Cc1ccccc1
|
| ZINC163130 | 0.560 | 232.3 Da LogP 2.66 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)c1ccccc1
|
| ZINC196676626 | 0.560 | 340.4 Da LogP 1.14 TPSA 92.3 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)NNS(=O)(=O)Cc1ccccc1
|
| ZINC399776 | 0.560 | 336.4 Da LogP 2.69 TPSA 68.3 | ✓ Ro5 | ✓ Clean |
O=S(=O)(/C=C/S(=O)(=O)Cc1ccccc1)Cc1ccccc1
|
| ZINC145170179 | 0.556 | 250.3 Da LogP 0.48 TPSA 88.5 | ✓ Ro5 | ✓ Clean |
CS(=O)(=O)c1ccc(CS(=O)(=O)O)cc1
|
| ZINC1713408 | 0.556 | 214.2 Da LogP 0.69 TPSA 71.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CS(=O)(=O)Cc1ccccc1
|
| ZINC255190110 | 0.556 | 386.5 Da LogP 3.63 TPSA 68.3 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)c1cccc(S(=O)(=O)Cc2ccccc2)c1
|
| ZINC26478554 | 0.556 | 200.3 Da LogP 0.59 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(CCO)Cc1ccccc1
|
| ZINC35058157 | 0.552 | 261.3 Da LogP 2.38 TPSA 60.2 | ✓ Ro5 | ✓ Clean |
Nc1cccc(CS(=O)(=O)Cc2ccccc2)c1
|
| ZINC14093286 | 0.538 | 368.5 Da LogP 1.23 TPSA 92.3 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)NCCNS(=O)(=O)Cc1ccccc1
|
| ZINC1163467 | 0.536 | 436.6 Da LogP 4.79 TPSA 68.3 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)c1cccc2c(S(=O)(=O)Cc3ccccc3)c…
|
| ZINC2509149 | 0.531 | 211.4 Da LogP 4.27 TPSA 12.0 | ✓ Ro5 | ✓ Clean |
CCCCCCCCNC1CCCCC1
|
| ZINC32929750 | 0.531 | 289.4 Da LogP 1.90 TPSA 77.2 | ✓ Ro5 | ✓ Clean |
NC(=O)c1cccc(CS(=O)(=O)Cc2ccccc2)c1
|
| ZINC130127586 | 0.529 | 260.4 Da LogP 1.38 TPSA 58.2 | ✓ Ro5 | ✓ Clean |
O=S(=O)(NCCNC1CCCCCC1)C1CC1
|
| ZINC143515753 | 0.519 | 200.3 Da LogP 1.64 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CCc1ccccc1CS(=O)(=O)O
|
| ZINC19367005 | 0.519 | 224.4 Da LogP 2.83 TPSA 24.1 | ✓ Ro5 | ✓ Clean |
C1CCC(NCCNC2CCCCC2)CC1
|
| ZINC29840 | 0.519 | 261.3 Da LogP 2.31 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)NCc1ccccc1
|
| ZINC45069273 | 0.519 | 273.6 Da LogP 2.93 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)C(Cl)(Cl)Cl
|
| ZINC12805654 | 0.517 | 444.6 Da LogP 2.93 TPSA 92.3 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)NCc1cccc(CNS(=O)(=O)Cc2ccccc2…
|
| ZINC13808031 | 0.517 | 213.3 Da LogP -0.21 TPSA 98.5 | ✓ Ro5 | ✓ Clean |
NC(N)=NS(=O)(=O)Cc1ccccc1
|
| ZINC1561883 | 0.517 | 229.3 Da LogP 0.19 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
O=C(O)CNS(=O)(=O)Cc1ccccc1
|
| ZINC1641128 | 0.517 | 242.3 Da LogP 2.68 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)CCCCCCc1ccccc1
|
| ZINC17021092 | 0.517 | 228.3 Da LogP 1.07 TPSA 71.4 | ✓ Ro5 | ✓ Clean |
C[C@H](C(=O)O)S(=O)(=O)Cc1ccccc1
|
| ZINC1704442 | 0.517 | 228.3 Da LogP 1.07 TPSA 71.4 | ✓ Ro5 | ✓ Clean |
C[C@@H](C(=O)O)S(=O)(=O)Cc1ccccc1
|
| ZINC1764786 | 0.517 | 217.2 Da LogP 0.98 TPSA 97.5 | ✓ Ro5 | ✓ Clean |
O=[N+]([O-])c1ccc(CS(=O)(=O)O)cc1
|
| ZINC3219150 | 0.517 | 263.3 Da LogP 2.41 TPSA 57.6 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)N(O)c1ccccc1
|
| ZINC4512996 | 0.517 | 228.3 Da LogP 1.08 TPSA 71.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CCS(=O)(=O)Cc1ccccc1
|
| ZINC65593788 | 0.517 | 274.4 Da LogP 3.42 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
Cc1cc(C)cc(CS(=O)(=O)Cc2ccccc2)c1
|
| ZINC78978926 | 0.516 | 266.7 Da LogP 3.31 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)c1cccc(Cl)c1
|
| ZINC96191894 | 0.516 | 217.2 Da LogP 0.98 TPSA 97.5 | ✓ Ro5 | ✓ Clean |
O=[N+]([O-])c1cccc(CS(=O)(=O)O)c1
|
| ZINC1641137 | 0.500 | 222.3 Da LogP 2.23 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)Cc1cccc2ccccc12
|
| ZINC1672446 | 0.500 | 228.3 Da LogP 1.49 TPSA 75.3 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCCCNC1CCCCC1)C(=O)O
|
| ZINC1926248 | 0.500 | 416.5 Da LogP 3.57 TPSA 92.3 | ✓ Ro5 | Alert |
O=S(=O)(Cc1ccccc1)Nc1ccc(NS(=O)(=O)Cc2ccccc2)cc1
|
| ZINC2168583 | 0.500 | 237.3 Da LogP 0.16 TPSA 86.6 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)C[C@@H](O)CNC1CCCCC1
|
| ZINC2168584 | 0.500 | 237.3 Da LogP 0.16 TPSA 86.6 | ✓ Ro5 | ✓ Clean |
O=S(=O)(O)C[C@H](O)CNC1CCCCC1
|
| ZINC236994621 | 0.500 | 290.4 Da LogP 0.85 TPSA 75.3 | ✓ Ro5 | ✓ Clean |
CCS(=O)(=O)CC(=O)NCCNC1CCCCCC1
|
| ZINC29852 | 0.500 | 247.3 Da LogP 2.63 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)Nc1ccccc1
|
| ZINC399887 | 0.500 | 274.3 Da LogP 2.48 TPSA 51.2 | ✓ Ro5 | ✓ Clean |
O=C(CS(=O)(=O)Cc1ccccc1)c1ccccc1
|
| ZINC44655186 | 0.500 | 213.4 Da LogP 3.12 TPSA 21.3 | ✓ Ro5 | ✓ Clean |
COCCCCNC1CCCCCCC1
|
| ZINC5840523 | 0.500 | 228.3 Da LogP 1.49 TPSA 75.3 | ✓ Ro5 | ✓ Clean |
N[C@H](CCCCNC1CCCCC1)C(=O)O
|
| ZINC65593700 | 0.500 | 314.3 Da LogP 3.82 TPSA 34.1 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)Cc1cccc(C(F)(F)F)c1
|
| ZINC728426 | 0.500 | 351.5 Da LogP 4.22 TPSA 37.4 | ✓ Ro5 | ✓ Clean |
O=S(=O)(Cc1ccccc1)N(Cc1ccccc1)Cc1ccccc1
|
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.