Amino acids
366
Annotations
8
Features
26
PDB binders
19
Druggability
0.232
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_00049
- Gene
- dnaN AHE41973.1
- Status
- annotated
- Amino acids
- 366
- Structure source
- AlphaFold + ColabFold
GO
GO:0009360 The DNA polymerase III holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential sub-assemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core carries out the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork.
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:0003887 Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 96.995
- DEG E-value
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 96.59
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.
FPocket
0.232
P2Rank
0.04
ColabFold model
Core conservation
Conserved core gene
Gut microbiome
164 / 4744
genomes with a hit
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
8 GO
Gene Ontology (GO)
8- GO:0009360 The DNA polymerase III holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential sub-assemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core carries out the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork.
- 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:0003887 Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
- 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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0042802 Binding to an identical protein or proteins.
- GO:0006271 The process in which an existing DNA strand is extended by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication.
Sequence Features
Domain/signature hits from InterPro and related databases.
26 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 248 | 366 | FunFam | G3DSA:3.10.150.10:FF:000003 | Beta sliding clamp |
| 1 | 365 | CDD | cd00140 | beta_clamp |
| 1 | 365 | InterPro | IPR001001 | DNA polymerase III, beta sliding clamp |
| 1 | 366 | PANTHER | PTHR30478 | DNA POLYMERASE III SUBUNIT BETA |
| 1 | 366 | InterPro | IPR001001 | DNA polymerase III, beta sliding clamp |
| 17 | 362 | SMART | SM00480 | pol35 |
| 17 | 362 | InterPro | IPR001001 | DNA polymerase III, beta sliding clamp |
| 1 | 366 | PIRSF | PIRSF000804 | DNA_pol_III_b |
| 1 | 121 | SUPERFAMILY | SSF55979 | DNA clamp |
| 1 | 121 | InterPro | IPR046938 | DNA clamp superfamily |
| 1 | 123 | FunFam | G3DSA:3.10.150.10:FF:000001 | Beta sliding clamp |
| 124 | 247 | Gene3D | G3DSA:3.10.150.10 | DNA Polymerase III, subunit A, domain 2 |
| 124 | 247 | FunFam | G3DSA:3.10.150.10:FF:000002 | Beta sliding clamp |
| 1 | 366 | NCBIfam | TIGR00663 | DNA polymerase III subunit beta |
| 129 | 243 | Pfam | PF02767 | DNA polymerase III beta subunit, central domain |
| 129 | 243 | InterPro | IPR022637 | DNA polymerase III, beta sliding clamp, central |
| 1 | 120 | Pfam | PF00712 | DNA polymerase III beta subunit, N-terminal domain |
| 1 | 120 | InterPro | IPR022634 | DNA polymerase III, beta sliding clamp, N-terminal |
| 245 | 366 | SUPERFAMILY | SSF55979 | DNA clamp |
| 245 | 366 | InterPro | IPR046938 | DNA clamp superfamily |
| 248 | 366 | Gene3D | G3DSA:3.10.150.10 | DNA Polymerase III, subunit A, domain 2 |
| 1 | 123 | Gene3D | G3DSA:3.10.150.10 | DNA Polymerase III, subunit A, domain 2 |
| 125 | 244 | SUPERFAMILY | SSF55979 | DNA clamp |
| 125 | 244 | InterPro | IPR046938 | DNA clamp superfamily |
| 245 | 365 | Pfam | PF02768 | DNA polymerase III beta subunit, C-terminal domain |
| 245 | 365 | InterPro | IPR022635 | DNA polymerase III, beta sliding clamp, C-terminal |
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...
Legend
High
Medium
Low
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_A0A0H3GV83
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_00049
|
ColabFold | — | — | full sequence | — | Loaded |
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 |
|---|---|---|---|---|---|---|---|
| 15 | 0.232 |
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 | 0.62 | 0.0 |
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 |
|---|---|---|---|---|---|---|---|
| 7 | 0.617 | ||||||
| 9 | 0.376 |
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 | 0.83 | 0.003 |
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.
74 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 |
|---|---|---|---|---|---|---|
| 0LA | P0A988 | 273.7 Da LogP 4.16 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
C[C@@H](c1ccc2c3cc(ccc3[nH]c2c1)Cl)C(=O)O
|
|
| 1FL | O25242 | 250.2 Da LogP 3.04 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
c1cc(c(cc1c2ccc(cc2F)F)C(=O)O)O
|
|
| 27O | P0A988 | 282.4 Da LogP 5.08 TPSA 37.3 | 1 viol. | ✓ Clean |
C[C@H](c1ccc(c2c1cccc2)C3CCCCC3)C(=O)O
|
|
| 27R | P0A988 | 334.2 Da LogP 2.89 TPSA 80.4 | ✓ Ro5 | Alert |
c1cc(c(c(c1)C(=O)c2ccc(cc2)Br)N)CC(=O)O
|
|
| 2HO | P0A988 | 157.1 Da LogP 1.06 TPSA 43.1 | ✓ Ro5 | ✓ Clean |
c1cc(c(cc1C(=O)N)F)F
|
|
| 2HQ | P0A988 | 181.6 Da LogP 1.47 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
c1cc2c(cc1Cl)C(=O)C(=O)N2
|
|
| 2HU | P0A988 | 162.1 Da LogP 2.08 TPSA 58.9 | ✓ Ro5 | ✓ Clean |
c1cc2c(cc[nH]2)cc1[N+](=O)[O-]
|
|
| 2J1 | P0A988 | 249.7 Da LogP 3.40 TPSA 53.1 | ✓ Ro5 | Alert |
c1c2c(cc(c1Cl)C(=O)O)[nH]c3c2CCCC3
|
|
| 2J2 | P0A988 | 249.7 Da LogP 3.33 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
c1cc2c(cc1Cl)c3c([nH]2)[C@@H](CCC3)C(=O)O
|
|
| 322 | P0A988 | 499.2 Da LogP 3.17 TPSA 87.1 | ✓ Ro5 | Alert |
CCOc1cc(c(c(c1O)Br)Br)C[C@@H]2C(=O)N(C(=S)S2)CC…
|
|
| 323 | P0A988 | 414.5 Da LogP 2.48 TPSA 76.6 | ✓ Ro5 | ✓ Clean |
CN(C)c1ccc2c(c1)OC3=CC(=[N+](C)C)C=CC3=C2c4ccc(…
|
|
| 4FC | P0A988 | 216.2 Da LogP 3.19 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
c1cc(ccc1c2ccc(cc2)F)C(=O)O
|
|
| 5CY | P0A988 | 471.7 Da LogP 5.62 TPSA 46.7 | 1 viol. | ✓ Clean |
CC1(c2ccccc2[N+](=C1/C=C/C=C/C=C/3\C(c4ccccc4N3…
|
|
| 6NI | P0A988 | 163.1 Da LogP 1.47 TPSA 71.8 | ✓ Ro5 | ✓ Clean |
c1cc2cn[nH]c2cc1[N+](=O)[O-]
|
|
| 743 | P0A988 | 434.5 Da LogP 5.49 TPSA 79.5 | 1 viol. | ✓ Clean |
CCCC(=NOCc1ccc(cc1)c2ccc(cc2)F)C3C(=O)CC(C(C3=O…
|
|
| BU3 | P9WNU1 | 90.1 Da LogP -0.25 TPSA 40.5 | ✓ Ro5 | ✓ Clean |
C[C@H]([C@@H](C)O)O
|
|
| MLU | P9WNU1 | 145.2 Da LogP 0.71 TPSA 49.3 | ✓ Ro5 | ✓ Clean |
CC(C)C[C@H](C(=O)O)NC
|
|
| P4C | P0A988 | 324.4 Da LogP -0.72 TPSA 92.7 | ✓ Ro5 | ✓ Clean |
C(COCCOCCOCCOCCOCCOCC=O)O
|
|
| SFK | P0A988 | 263.3 Da LogP 2.23 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(C)CCC(=O)N[C@@H](Cc1ccccc1)C(=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).
| Ligand | UniProt (homolog) | pchembl | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| CHEMBL3577268 | P0A988 | — | 249.7 Da LogP 3.01 TPSA 53.1 | ✓ Ro5 | Alert |
O=C(O)[C@@H]1CCc2c([nH]c3ccc(Cl)cc23)C1
|
| CHEMBL3577269 | P0A988 | — | 249.7 Da LogP 3.01 TPSA 53.1 | ✓ Ro5 | Alert |
O=C(O)[C@H]1CCc2c([nH]c3ccc(Cl)cc23)C1
|
| CHEMBL3577272 | P0A988 | — | 294.1 Da LogP 3.12 TPSA 53.1 | ✓ Ro5 | Alert |
O=C(O)[C@@H]1CCc2c([nH]c3ccc(Br)cc23)C1
|
| CHEMBL3577289 | P0A988 | — | 499.4 Da LogP 3.41 TPSA 108.6 | ✓ Ro5 | Alert |
O=C(Cn1c2c(c3cc(Br)ccc31)CC[C@@H](C(=O)O)C2)N[C…
|
| CHEMBL3577290 | P0A988 | — | 499.4 Da LogP 3.41 TPSA 108.6 | ✓ Ro5 | Alert |
O=C(Cn1c2c(c3cc(Br)ccc31)CC[C@@H](C(=O)O)C2)N[C…
|
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 |
|---|---|---|---|---|---|
| ZINC117391805 | 1.000 | 294.1 Da LogP 3.12 TPSA 53.1 | ✓ Ro5 | Alert |
O=C(O)[C@@H]1CCc2c([nH]c3ccc(Br)cc23)C1
|
| ZINC117391807 | 1.000 | 294.1 Da LogP 3.12 TPSA 53.1 | ✓ Ro5 | Alert |
O=C(O)[C@H]1CCc2c([nH]c3ccc(Br)cc23)C1
|
| ZINC1869694 | 1.000 | 273.7 Da LogP 4.16 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
C[C@@H](C(=O)O)c1ccc2c(c1)[nH]c1ccc(Cl)cc12
|
| ZINC20235 | 1.000 | 273.7 Da LogP 4.16 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
C[C@H](C(=O)O)c1ccc2c(c1)[nH]c1ccc(Cl)cc12
|
| ZINC20249400 | 1.000 | 263.3 Da LogP 2.23 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(C)CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC20249402 | 1.000 | 263.3 Da LogP 2.23 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(C)CCC(=O)N[C@H](Cc1ccccc1)C(=O)O
|
| ZINC2382451 | 1.000 | 216.2 Da LogP 3.19 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(-c2ccc(F)cc2)cc1
|
| ZINC2570817 | 1.000 | 334.2 Da LogP 2.89 TPSA 80.4 | ✓ Ro5 | Alert |
Nc1c(CC(=O)O)cccc1C(=O)c1ccc(Br)cc1
|
| ZINC340258 | 1.000 | 249.7 Da LogP 3.33 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1CCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC4018831 | 1.000 | 249.7 Da LogP 3.33 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@@H]1CCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC807911 | 1.000 | 249.7 Da LogP 3.40 TPSA 53.1 | ✓ Ro5 | Alert |
O=C(O)c1cc2[nH]c3c(c2cc1Cl)CCCC3
|
| ZINC575319668 | 0.923 | 263.7 Da LogP 3.72 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1CCCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC575319669 | 0.923 | 263.7 Da LogP 3.72 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@@H]1CCCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC49837746 | 0.810 | 249.7 Da LogP 3.01 TPSA 53.1 | ✓ Ro5 | Alert |
O=C(O)[C@H]1CCc2[nH]c3ccc(Cl)cc3c2C1
|
| ZINC49837747 | 0.810 | 249.7 Da LogP 3.01 TPSA 53.1 | ✓ Ro5 | Alert |
O=C(O)[C@@H]1CCc2[nH]c3ccc(Cl)cc3c2C1
|
| ZINC93985 | 0.786 | 248.7 Da LogP 2.73 TPSA 58.9 | ✓ Ro5 | ✓ Clean |
NC(=O)[C@H]1CCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC93989 | 0.786 | 248.7 Da LogP 2.73 TPSA 58.9 | ✓ Ro5 | ✓ Clean |
NC(=O)[C@@H]1CCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC909 | 0.765 | 255.3 Da LogP 2.13 TPSA 80.4 | ✓ Ro5 | Alert |
Nc1c(CC(=O)O)cccc1C(=O)c1ccccc1
|
| ZINC11891070 | 0.750 | 249.3 Da LogP 1.84 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(C)CC(=O)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC11891072 | 0.750 | 249.3 Da LogP 1.84 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CC(C)CC(=O)N[C@H](Cc1ccccc1)C(=O)O
|
| ZINC134079 | 0.750 | 242.2 Da LogP 2.75 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(-c2ccc(C(=O)O)cc2)cc1
|
| ZINC3147211 | 0.750 | 318.3 Da LogP 4.42 TPSA 74.6 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(-c2ccc(-c3ccc(C(=O)O)cc3)cc2)cc1
|
| ZINC15261553 | 0.737 | 294.3 Da LogP -0.01 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@H](CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O)C(=O)O
|
| ZINC15261555 | 0.737 | 294.3 Da LogP -0.01 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)N[C@H](Cc1ccccc1)C(=O)O)C(=O)O
|
| ZINC15261557 | 0.737 | 294.3 Da LogP -0.01 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@H](CCC(=O)N[C@H](Cc1ccccc1)C(=O)O)C(=O)O
|
| ZINC2242693 | 0.737 | 294.3 Da LogP -0.01 TPSA 129.7 | ✓ Ro5 | ✓ Clean |
N[C@@H](CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O)C(=O)O
|
| ZINC16946243 | 0.733 | 257.7 Da LogP 3.14 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
O=C1Nc2ccc(-c3ccc(Cl)cc3)cc2C1=O
|
| ZINC53542 | 0.733 | 263.7 Da LogP 3.41 TPSA 42.1 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@H]1CCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC53543 | 0.733 | 263.7 Da LogP 3.41 TPSA 42.1 | ✓ Ro5 | ✓ Clean |
COC(=O)[C@@H]1CCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC5161668 | 0.730 | 289.7 Da LogP 2.78 TPSA 80.4 | ✓ Ro5 | Alert |
Nc1c(CC(=O)O)cccc1C(=O)c1ccc(Cl)cc1
|
| ZINC499303 | 0.727 | 262.7 Da LogP 3.12 TPSA 58.9 | ✓ Ro5 | ✓ Clean |
NC(=O)[C@H]1CCCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC499304 | 0.727 | 262.7 Da LogP 3.12 TPSA 58.9 | ✓ Ro5 | ✓ Clean |
NC(=O)[C@@H]1CCCCc2c1[nH]c1ccc(Cl)cc21
|
| ZINC1598043 | 0.722 | 236.3 Da LogP 0.15 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
NCCC(=O)N[C@H](Cc1ccccc1)C(=O)O
|
| ZINC1845204 | 0.722 | 297.4 Da LogP 2.43 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=C(CCc1ccccc1)N[C@H](Cc1ccccc1)C(=O)O
|
| ZINC1845206 | 0.722 | 297.4 Da LogP 2.43 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
O=C(CCc1ccccc1)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC2545129 | 0.722 | 236.3 Da LogP 0.15 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
NCCC(=O)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC3175547 | 0.722 | 265.3 Da LogP 0.66 TPSA 103.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC3175549 | 0.722 | 265.3 Da LogP 0.66 TPSA 103.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CCC(=O)N[C@H](Cc1ccccc1)C(=O)O
|
| ZINC128690 | 0.721 | 294.1 Da LogP 3.43 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@H]1CCCc2c1[nH]c1ccc(Br)cc21
|
| ZINC128692 | 0.721 | 294.1 Da LogP 3.43 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
O=C(O)[C@@H]1CCCc2c1[nH]c1ccc(Br)cc21
|
| ZINC3683849 | 0.721 | 229.3 Da LogP 2.98 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
Cc1ccc2[nH]c3c(c2c1)CCC[C@@H]3C(=O)O
|
| ZINC3683850 | 0.721 | 229.3 Da LogP 2.98 TPSA 53.1 | ✓ Ro5 | ✓ Clean |
Cc1ccc2[nH]c3c(c2c1)CCC[C@H]3C(=O)O
|
| ZINC2513032 | 0.720 | 234.2 Da LogP 3.33 TPSA 37.3 | ✓ Ro5 | ✓ Clean |
O=C(O)c1ccc(-c2cc(F)cc(F)c2)cc1
|
| ZINC1677646 | 0.714 | 221.3 Da LogP 1.21 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CCC(=O)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC6655209 | 0.714 | 221.3 Da LogP 1.21 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CCC(=O)N[C@H](Cc1ccccc1)C(=O)O
|
| ZINC22054172 | 0.711 | 301.8 Da LogP 4.64 TPSA 42.1 | ✓ Ro5 | ✓ Clean |
CCOC(=O)[C@@H](C)c1ccc2c(c1)[nH]c1ccc(Cl)cc12
|
| ZINC22054176 | 0.711 | 301.8 Da LogP 4.64 TPSA 42.1 | ✓ Ro5 | ✓ Clean |
CCOC(=O)[C@H](C)c1ccc2c(c1)[nH]c1ccc(Cl)cc12
|
| ZINC11891064 | 0.711 | 249.3 Da LogP 1.99 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CCCCC(=O)N[C@@H](Cc1ccccc1)C(=O)O
|
| ZINC11891067 | 0.711 | 249.3 Da LogP 1.99 TPSA 66.4 | ✓ Ro5 | ✓ Clean |
CCCCC(=O)N[C@H](Cc1ccccc1)C(=O)O
|
| ZINC757568599 | 0.704 | 233.2 Da LogP 2.73 TPSA 43.1 | ✓ Ro5 | ✓ Clean |
NC(=O)c1ccc(-c2ccc(F)c(F)c2)cc1
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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.