Overview
Basic information about this protein and its source genome.
- Accession
- PA4281
- Gene
- PA4281 sbcD
- Status
- annotated
- Amino acids
- 409
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- Cytoplasmic
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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
9- GO:0008408 Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
- GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0004529 Catalysis of the sequential cleavage of mononucleotides from a free 5' or 3' terminus of a DNA molecule.
- GO:0004519 Catalysis of the cleavage of ester linkages within nucleic acids by creating internal breaks.
- GO:0006310 Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
- GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
- GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
- GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
- GO:0006259 Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 344 | SUPERFAMILY | SSF56300 | Metallo-dependent phosphatases |
| 1 | 344 | InterPro | IPR029052 | Metallo-dependent phosphatase-like |
| 284 | 378 | Pfam | PF12320 | Type 5 capsule protein repressor C-terminal domain |
| 284 | 378 | InterPro | IPR026843 | Nuclease SbcCD subunit D, C-terminal domain |
| 1 | 257 | NCBIfam | TIGR00619 | exonuclease subunit SbcD |
| 1 | 257 | InterPro | IPR004593 | Nuclease SbcCD subunit D |
| 1 | 280 | Gene3D | G3DSA:3.60.21.10 | - |
| 1 | 280 | InterPro | IPR029052 | Metallo-dependent phosphatase-like |
| 1 | 403 | PANTHER | PTHR30337 | COMPONENT OF ATP-DEPENDENT DSDNA EXONUCLEASE |
| 1 | 231 | Pfam | PF00149 | Calcineurin-like phosphoesterase |
| 1 | 231 | InterPro | IPR004843 | Calcineurin-like phosphoesterase domain, ApaH type |
| 2 | 251 | CDD | cd00840 | MPP_Mre11_N |
| 2 | 251 | InterPro | IPR041796 | Mre11 nuclease, N-terminal metallophosphatase domain |
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 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA4281
|
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 |
|---|---|---|---|---|---|---|---|
| 4 | 0.595 | ||||||
| 1 | 0.356 |
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 |
|---|---|---|---|---|---|---|
| 2PK | Q9X1X0 | 220.3 Da LogP 1.53 TPSA 73.2 | ✓ Ro5 | ✓ Clean |
[H]/N=C\1/NC(=O)/C(=C\c2ccc(cc2)O)/S1
|
|
| 2PV | Q9X1X0 | 219.3 Da LogP 1.41 TPSA 79.0 | ✓ Ro5 | ✓ Clean |
[H]/N=C\1/NC(=O)/C(=C\c2ccc(cc2)N)/S1
|
|
| 2PW | Q9X1X0 | 293.4 Da LogP 3.39 TPSA 40.5 | ✓ Ro5 | Alert |
CC[C@@H](C)N1C(=O)/C(=C\c2ccc(cc2)O)/SC1=S
|
|
| 2Q0 | Q9X1X0 | 293.4 Da LogP 3.25 TPSA 40.5 | ✓ Ro5 | Alert |
CC(C)CN1C(=O)/C(=C/c2ccc(cc2)O)/SC1=S
|
|
| BU7 | Q9X1X0 | 293.4 Da LogP 3.39 TPSA 40.5 | ✓ Ro5 | Alert |
CCCCN1C(=O)/C(=C\c2ccc(cc2)O)/SC1=S
|
|
| UKV | Q9X1X0 | 251.3 Da LogP 2.18 TPSA 38.3 | ✓ Ro5 | Alert |
COc1cccc(c1)/C=C\2/C(=O)NC(=S)S2
|
|
| UL1 | Q9X1X0 | 281.4 Da LogP 2.19 TPSA 47.6 | ✓ Ro5 | Alert |
COc1ccc(cc1OC)/C=C\2/C(=O)NC(=S)S2
|
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 |
|---|---|---|---|---|---|
| ZINC2293110020 | 1.000 | 293.4 Da LogP 3.25 TPSA 40.5 | ✓ Ro5 | Alert |
CC(C)CN1C(=O)C(=Cc2ccc(O)cc2)SC1=S
|
| ZINC2672553 | 1.000 | 293.4 Da LogP 3.39 TPSA 40.5 | ✓ Ro5 | Alert |
CCCCN1C(=O)/C(=C/c2ccc(O)cc2)SC1=S
|
| ZINC2707200 | 1.000 | 293.4 Da LogP 3.25 TPSA 40.5 | ✓ Ro5 | Alert |
CC(C)CN1C(=O)/C(=C/c2ccc(O)cc2)SC1=S
|
| ZINC4815953 | 1.000 | 293.4 Da LogP 3.39 TPSA 40.5 | ✓ Ro5 | Alert |
CCCCN1C(=O)/C(=C\c2ccc(O)cc2)SC1=S
|
| ZINC5497857 | 1.000 | 293.4 Da LogP 3.25 TPSA 40.5 | ✓ Ro5 | Alert |
CC(C)CN1C(=O)/C(=C\c2ccc(O)cc2)SC1=S
|
| ZINC2572998 | 0.925 | 307.4 Da LogP 3.78 TPSA 40.5 | ✓ Ro5 | Alert |
CCCCCN1C(=O)/C(=C/c2ccc(O)cc2)SC1=S
|
| ZINC2666879 | 0.902 | 321.5 Da LogP 4.17 TPSA 40.5 | ✓ Ro5 | Alert |
CCCCCCN1C(=O)/C(=C/c2ccc(O)cc2)SC1=S
|
| ZINC5502031 | 0.902 | 321.5 Da LogP 4.17 TPSA 40.5 | ✓ Ro5 | Alert |
CCCCCCN1C(=O)/C(=C\c2ccc(O)cc2)SC1=S
|
| ZINC1162232 | 0.872 | 279.4 Da LogP 3.00 TPSA 40.5 | ✓ Ro5 | Alert |
CCCN1C(=O)/C(=C/c2ccc(O)cc2)SC1=S
|
| ZINC13940186 | 0.841 | 387.5 Da LogP 3.64 TPSA 56.8 | ✓ Ro5 | Alert |
COc1cccc(OCCOc2cccc(/C=C3\SC(=S)NC3=O)c2)c1
|
| ZINC2961441 | 0.841 | 387.5 Da LogP 3.64 TPSA 56.8 | ✓ Ro5 | Alert |
COc1cccc(OCCOc2cccc(/C=C3/SC(=S)NC3=O)c2)c1
|
| ZINC2873978 | 0.822 | 401.5 Da LogP 4.03 TPSA 56.8 | ✓ Ro5 | Alert |
COc1cccc(OCCCOc2cccc(/C=C3/SC(=S)NC3=O)c2)c1
|
| ZINC12600413 | 0.814 | 309.4 Da LogP 2.97 TPSA 47.6 | ✓ Ro5 | Alert |
COc1cc(/C=C2\SC(=S)NC2=O)ccc1OC(C)C
|
| ZINC12690557 | 0.814 | 295.4 Da LogP 2.58 TPSA 47.6 | ✓ Ro5 | Alert |
CCOc1cc(/C=C2\SC(=S)NC2=O)ccc1OC
|
| ZINC13556347 | 0.814 | 295.4 Da LogP 2.58 TPSA 47.6 | ✓ Ro5 | Alert |
CCOc1ccc(/C=C2\SC(=S)NC2=O)cc1OC
|
| ZINC2988006 | 0.814 | 345.4 Da LogP 1.52 TPSA 81.7 | ✓ Ro5 | Alert |
COc1cc(/C=C2/SC(=S)NC2=O)ccc1OS(C)(=O)=O
|
| ZINC12600066 | 0.805 | 265.4 Da LogP 2.49 TPSA 38.3 | ✓ Ro5 | Alert |
COc1ccc(/C=C2\SC(=S)NC2=O)cc1C
|
| ZINC13942008 | 0.800 | 417.5 Da LogP 3.65 TPSA 66.0 | ✓ Ro5 | Alert |
COc1ccccc1OCCOc1ccc(/C=C2\SC(=S)NC2=O)cc1OC
|
| ZINC168930704 | 0.800 | 219.3 Da LogP 1.41 TPSA 79.0 | ✓ Ro5 | ✓ Clean |
N=C1NC(=O)/C(=C/c2ccc(N)cc2)S1
|
| ZINC2038176995 | 0.800 | 220.3 Da LogP 1.53 TPSA 73.2 | ✓ Ro5 | ✓ Clean |
N=C1NC(=O)C(=Cc2ccc(O)cc2)S1
|
| ZINC4473160 | 0.800 | 220.3 Da LogP 1.53 TPSA 73.2 | ✓ Ro5 | ✓ Clean |
N=C1NC(=O)/C(=C\c2ccc(O)cc2)S1
|
| ZINC15135173 | 0.795 | 309.4 Da LogP 2.11 TPSA 64.6 | ✓ Ro5 | Alert |
COc1cc(/C=C2\SC(=S)NC2=O)ccc1OC(C)=O
|
| ZINC1164392 | 0.791 | 295.4 Da LogP 3.83 TPSA 20.3 | ✓ Ro5 | Alert |
CC[C@@H](C)N1C(=O)/C(=C/c2ccc(F)cc2)SC1=S
|
| ZINC1164394 | 0.791 | 295.4 Da LogP 3.83 TPSA 20.3 | ✓ Ro5 | Alert |
CC[C@H](C)N1C(=O)/C(=C/c2ccc(F)cc2)SC1=S
|
| ZINC1165147 | 0.791 | 356.3 Da LogP 4.45 TPSA 20.3 | ✓ Ro5 | Alert |
CC[C@@H](C)N1C(=O)/C(=C/c2ccc(Br)cc2)SC1=S
|
| ZINC1165149 | 0.791 | 356.3 Da LogP 4.45 TPSA 20.3 | ✓ Ro5 | Alert |
CC[C@H](C)N1C(=O)/C(=C/c2ccc(Br)cc2)SC1=S
|
| ZINC1031760 | 0.786 | 377.2 Da LogP 2.79 TPSA 38.3 | ✓ Ro5 | Alert |
COc1ccc(/C=C2/SC(=S)NC2=O)cc1I
|
| ZINC1182221 | 0.786 | 291.4 Da LogP 3.85 TPSA 20.3 | ✓ Ro5 | Alert |
Cc1ccc(/C=C2/SC(=S)N(CC(C)C)C2=O)cc1
|
| ZINC1182222 | 0.786 | 291.4 Da LogP 3.85 TPSA 20.3 | ✓ Ro5 | Alert |
Cc1ccc(/C=C2\SC(=S)N(CC(C)C)C2=O)cc1
|
| ZINC15163070 | 0.786 | 377.2 Da LogP 2.79 TPSA 38.3 | ✓ Ro5 | Alert |
COc1ccc(/C=C2\SC(=S)NC2=O)cc1I
|
| ZINC1857623806 | 0.786 | 267.3 Da LogP 1.89 TPSA 58.6 | ✓ Ro5 | Alert |
COc1cc(C=C2SC(=S)NC2=O)ccc1O
|
| ZINC2706865 | 0.786 | 291.4 Da LogP 4.00 TPSA 20.3 | ✓ Ro5 | Alert |
CCCCN1C(=O)/C(=C/c2ccc(C)cc2)SC1=S
|
| ZINC35042128 | 0.786 | 277.3 Da LogP 3.23 TPSA 57.6 | ✓ Ro5 | ✓ Clean |
CCCCN1C(=O)S/C(=C/c2ccc(O)cc2)C1=O
|
| ZINC5503600 | 0.786 | 291.4 Da LogP 4.00 TPSA 20.3 | ✓ Ro5 | Alert |
CCCCN1C(=O)/C(=C\c2ccc(C)cc2)SC1=S
|
| ZINC5552373 | 0.786 | 277.3 Da LogP 3.23 TPSA 57.6 | ✓ Ro5 | ✓ Clean |
CCCCN1C(=O)S/C(=C\c2ccc(O)cc2)C1=O
|
| ZINC15857056 | 0.783 | 431.5 Da LogP 4.04 TPSA 66.0 | ✓ Ro5 | Alert |
COc1ccccc1OCCCOc1ccc(/C=C2/SC(=S)NC2=O)cc1OC
|
| ZINC5102380 | 0.783 | 387.5 Da LogP 3.64 TPSA 56.8 | ✓ Ro5 | Alert |
COc1ccc(OCCOc2cccc(/C=C3\SC(=S)NC3=O)c2)cc1
|
| ZINC1233033 | 0.780 | 265.4 Da LogP 2.61 TPSA 40.5 | ✓ Ro5 | Alert |
CCN1C(=O)/C(=C/c2ccc(O)cc2)SC1=S
|
| ZINC4477965 | 0.780 | 265.4 Da LogP 2.61 TPSA 40.5 | ✓ Ro5 | Alert |
CCN1C(=O)/C(=C\c2ccc(O)cc2)SC1=S
|
| ZINC13563168 | 0.778 | 309.4 Da LogP 2.97 TPSA 47.6 | ✓ Ro5 | Alert |
CCCOc1ccc(/C=C2\SC(=S)NC2=O)cc1OC
|
| ZINC5128453 | 0.778 | 309.4 Da LogP 2.97 TPSA 47.6 | ✓ Ro5 | Alert |
CCCOc1cc(/C=C2\SC(=S)NC2=O)ccc1OC
|
| ZINC12529699 | 0.769 | 265.3 Da LogP 2.03 TPSA 64.6 | ✓ Ro5 | ✓ Clean |
COc1ccc(/C=C2\SC(=O)NC2=O)cc1OC
|
| ZINC1857622548 | 0.769 | 265.3 Da LogP 2.03 TPSA 64.6 | ✓ Ro5 | ✓ Clean |
COc1ccc(C=C2SC(=O)NC2=O)cc1OC
|
| ZINC9331564 | 0.769 | 265.3 Da LogP 2.03 TPSA 64.6 | ✓ Ro5 | ✓ Clean |
COc1ccc(/C=C2/SC(=O)NC2=O)cc1OC
|
| ZINC1117323 | 0.767 | 311.9 Da LogP 4.20 TPSA 20.3 | ✓ Ro5 | Alert |
CC(C)CN1C(=O)/C(=C/c2ccc(Cl)cc2)SC1=S
|
| ZINC1446656 | 0.767 | 319.5 Da LogP 4.67 TPSA 20.3 | ✓ Ro5 | Alert |
CC(C)CN1C(=O)/C(=C/c2ccc(C(C)C)cc2)SC1=S
|
| ZINC2706848 | 0.767 | 295.4 Da LogP 3.83 TPSA 20.3 | ✓ Ro5 | Alert |
CCCCN1C(=O)/C(=C/c2ccc(F)cc2)SC1=S
|
| ZINC4690374 | 0.767 | 356.3 Da LogP 4.45 TPSA 20.3 | ✓ Ro5 | Alert |
CCCCN1C(=O)/C(=C/c2ccc(Br)cc2)SC1=S
|
| ZINC4955214 | 0.767 | 311.9 Da LogP 4.34 TPSA 20.3 | ✓ Ro5 | Alert |
CCCCN1C(=O)/C(=C\c2ccc(Cl)cc2)SC1=S
|
| ZINC5497852 | 0.767 | 319.5 Da LogP 4.67 TPSA 20.3 | ✓ Ro5 | Alert |
CC(C)CN1C(=O)/C(=C\c2ccc(C(C)C)cc2)SC1=S
|
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.