Protein profile
KP13_04672
Phenylalanyl-tRNA synthetase beta chain
Genome: KpKP13
Amino acids
795
Annotations
8
Features
53
PDB binders
4
Druggability
0.821
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_04672
- Gene
- pheT AHE44068.1
- Status
- annotated
- Amino acids
- 795
- Structure source
- AlphaFold + ColabFold
EC
GO
GO:0004826 Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
GO:0000049 Binding to a transfer RNA.
GO:0006432 The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0003723 Binding to an RNA molecule or a portion thereof.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 22.716
- Human E-value
- 5.5e-10
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 92.453
- DEG E-value
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 95.58
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.
FPocket
0.821
P2Rank
0.876
ColabFold model
Core conservation
Conserved core gene
Gut microbiome
153 / 4744
genomes with a hit
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
7 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
7- GO:0004826 Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
- GO:0000049 Binding to a transfer RNA.
- GO:0006432 The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
- GO:0000287 Binding to a magnesium (Mg) ion.
- GO:0003723 Binding to an RNA molecule or a portion thereof.
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- GO:0009328 An enzyme complex that catalyzes the ligation of phenylalanine to tRNA(Phe), forming L-phenylalanyl-tRNA(Phe).
Sequence Features
Domain/signature hits from InterPro and related databases.
53 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 45 | 145 | Pfam | PF01588 | Putative tRNA binding domain |
| 45 | 145 | InterPro | IPR002547 | tRNA-binding domain |
| 1 | 788 | Hamap | MF_00283 | Phenylalanine--tRNA ligase beta subunit [pheT]. |
| 1 | 788 | InterPro | IPR004532 | Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type |
| 696 | 794 | SUPERFAMILY | SSF54991 | Anticodon-binding domain of PheRS |
| 696 | 794 | InterPro | IPR036690 | Ferrodoxin-fold anticodon-binding domain superfamily |
| 401 | 476 | ProSiteProfiles | PS51483 | B5 domain profile. |
| 401 | 476 | InterPro | IPR005147 | tRNA synthetase, B5-domain |
| 53 | 147 | CDD | cd02796 | tRNA_bind_bactPheRS |
| 53 | 147 | InterPro | IPR033714 | Phenylalanly tRNA synthetase, tRNA-binding-domain |
| 196 | 397 | FunFam | G3DSA:3.50.40.10:FF:000001 | Phenylalanine--tRNA ligase beta subunit |
| 475 | 685 | Pfam | PF17759 | Phenylalanyl tRNA synthetase beta chain CLM domain |
| 475 | 685 | InterPro | IPR041616 | Phenylalanyl tRNA synthetase beta chain, core domain |
| 404 | 475 | SUPERFAMILY | SSF46955 | Putative DNA-binding domain |
| 404 | 475 | InterPro | IPR009061 | Putative DNA-binding domain superfamily |
| 701 | 794 | Pfam | PF03147 | Ferredoxin-fold anticodon binding domain |
| 701 | 794 | InterPro | IPR005121 | Ferrodoxin-fold anticodon-binding domain |
| 403 | 471 | SMART | SM00874 | B5_2 |
| 403 | 471 | InterPro | IPR005147 | tRNA synthetase, B5-domain |
| 212 | 385 | SMART | SM00873 | B3_4_2 |
| 212 | 385 | InterPro | IPR005146 | B3/B4 tRNA-binding domain |
| 401 | 475 | Gene3D | G3DSA:3.30.56.10 | - |
| 702 | 795 | Gene3D | G3DSA:3.30.70.380 | - |
| 702 | 795 | InterPro | IPR036690 | Ferrodoxin-fold anticodon-binding domain superfamily |
| 485 | 693 | Gene3D | G3DSA:3.30.930.10 | Bira Bifunctional Protein; Domain 2 |
| 485 | 693 | InterPro | IPR045864 | Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) |
| 1 | 794 | NCBIfam | TIGR00472 | phenylalanine--tRNA ligase subunit beta |
| 1 | 794 | InterPro | IPR004532 | Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type |
| 702 | 795 | FunFam | G3DSA:3.30.70.380:FF:000001 | Phenylalanine--tRNA ligase beta subunit |
| 4 | 686 | PANTHER | PTHR10947 | PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47 |
| 4 | 686 | InterPro | IPR045060 | Phenylalanine-tRNA ligase, class IIc, beta subunit |
| 487 | 692 | FunFam | G3DSA:3.30.930.10:FF:000022 | Phenylalanine--tRNA ligase beta subunit |
| 467 | 690 | SUPERFAMILY | SSF55681 | Class II aaRS and biotin synthetases |
| 467 | 690 | InterPro | IPR045864 | Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) |
| 39 | 148 | ProSiteProfiles | PS50886 | tRNA-binding domain profile. |
| 39 | 148 | InterPro | IPR002547 | tRNA-binding domain |
| 7 | 180 | Gene3D | G3DSA:3.30.56.10 | - |
| 39 | 154 | Gene3D | G3DSA:2.40.50.140 | - |
| 39 | 154 | InterPro | IPR012340 | Nucleic acid-binding, OB-fold |
| 197 | 395 | Gene3D | G3DSA:3.50.40.10 | - |
| 197 | 395 | InterPro | IPR020825 | Phenylalanyl-tRNA synthetase-like, B3/B4 |
| 39 | 154 | FunFam | G3DSA:2.40.50.140:FF:000045 | Phenylalanine--tRNA ligase beta subunit |
| 35 | 197 | SUPERFAMILY | SSF50249 | Nucleic acid-binding proteins |
| 35 | 197 | InterPro | IPR012340 | Nucleic acid-binding, OB-fold |
| 195 | 396 | SUPERFAMILY | SSF56037 | PheT/TilS domain |
| 701 | 794 | SMART | SM00896 | FDX_ACB_2 |
| 402 | 475 | FunFam | G3DSA:3.30.56.10:FF:000002 | Phenylalanine--tRNA ligase beta subunit |
| 212 | 385 | Pfam | PF03483 | B3/4 domain |
| 406 | 471 | Pfam | PF03484 | tRNA synthetase B5 domain |
| 406 | 471 | InterPro | IPR005147 | tRNA synthetase, B5-domain |
| 701 | 794 | ProSiteProfiles | PS51447 | Ferredoxin-fold anticodon binding (FDX-ACB) domain profile. |
| 495 | 689 | CDD | cd00769 | PheRS_beta_core |
| 495 | 689 | InterPro | IPR041616 | Phenylalanyl tRNA synthetase beta chain, core 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...
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_A0A0H3GUX6
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_04672
|
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.821 | ||||||
| 3 | 0.475 | ||||||
| 32 | 0.232 | ||||||
| 6 | 0.227 |
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 | 13.84 | 0.701 | ||||||
| 2 | 7.84 | 0.416 | ||||||
| 3 | 2.77 | 0.084 | ||||||
| 4 | 2.6 | 0.075 | ||||||
| 5 | 1.95 | 0.041 |
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 |
|---|---|---|---|---|---|---|---|
| 2 | 0.566 |
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 | 12.29 | 0.646 | ||||||
| 2 | 7.13 | 0.37 | ||||||
| 3 | 1.99 | 0.042 | ||||||
| 4 | 1.95 | 0.041 | ||||||
| 5 | 1.49 | 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.
54 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 |
|---|---|---|---|---|---|---|
| DAH | P27002 | 197.2 Da LogP 0.05 TPSA 103.8 | ✓ Ro5 | Alert |
c1cc(c(cc1C[C@@H](C(=O)O)N)O)O
|
|
| MTY | Q5SGX1 | 181.2 Da LogP 0.35 TPSA 83.5 | ✓ Ro5 | ✓ Clean |
c1cc(cc(c1)O)C[C@@H](C(=O)O)N
|
|
| PUY | Q5SGX1 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
CN(C)c1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H]…
|
|
| TAM | Q7MXR4 | 163.2 Da LogP -1.17 TPSA 86.7 | ✓ Ro5 | ✓ Clean |
C(CO)C(CCO)(CCO)N
|
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 |
|---|---|---|---|---|---|
| ZINC53147178 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@@H…
|
| ZINC53147179 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@@H]…
|
| ZINC58994963 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@@H]…
|
| ZINC59065899 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](O)[C@@H](n…
|
| ZINC59817042 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@H](…
|
| ZINC59817043 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N[C@H]2[C@H](O)[C@@H](n3…
|
| ZINC59817045 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N[C@H]2[C@H](O)[C@H](n3c…
|
| ZINC61389312 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@H](…
|
| ZINC71789712 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@H]…
|
| ZINC73333306 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@H](n…
|
| ZINC73333309 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@@H](…
|
| ZINC73333313 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@H](N)C(=O)N[C@H]2[C@H](O)[C@@H](n3c…
|
| ZINC73333316 | 1.000 | 471.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
COc1ccc(C[C@H](N)C(=O)N[C@H]2[C@H](O)[C@H](n3cn…
|
| ZINC4830897 | 0.829 | 443.5 Da LogP -1.28 TPSA 183.7 | 1 viol. | ✓ Clean |
COc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@H](n…
|
| ZINC4830899 | 0.829 | 443.5 Da LogP -1.28 TPSA 183.7 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@H](…
|
| ZINC4830900 | 0.829 | 443.5 Da LogP -1.28 TPSA 183.7 | 1 viol. | ✓ Clean |
COc1ccc(C[C@H](N)C(=O)N[C@H]2[C@H](CO)O[C@H](n3…
|
| ZINC4830901 | 0.829 | 443.5 Da LogP -1.28 TPSA 183.7 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N[C@H]2[C@H](CO)O[C@H](n…
|
| ZINC1775953634 | 0.824 | 495.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
C#CCOc1ccc(C[C@H](N)C(=O)N[C@H]2[C@@H](CO)O[C@@…
|
| ZINC205891530 | 0.824 | 495.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
C#CCOc1ccc(C[C@H](N)C(=O)N[C@@H]2[C@@H](CO)O[C@…
|
| ZINC221530727 | 0.824 | 495.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
C#CCOc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](CO)O[C@…
|
| ZINC221530830 | 0.824 | 495.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
C#CCOc1ccc(C[C@@H](N)C(=O)N[C@H]2[C@H](O)[C@@H]…
|
| ZINC222589180 | 0.824 | 495.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
C#CCOc1ccc(C[C@H](N)C(=O)N[C@H]2[C@@H](CO)O[C@@…
|
| ZINC669678878 | 0.824 | 495.5 Da LogP -0.79 TPSA 160.9 | 1 viol. | ✓ Clean |
C#CCOc1ccc(C[C@@H](N)C(=O)N[C@@H]2[C@H](O)[C@@H…
|
| ZINC403598 | 0.800 | 273.3 Da LogP 2.14 TPSA 92.8 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O
|
| ZINC403599 | 0.800 | 273.3 Da LogP 2.14 TPSA 92.8 | ✓ Ro5 | ✓ Clean |
N[C@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O
|
| ZINC1834294 | 0.793 | 252.3 Da LogP -0.40 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1cccc(C[C@H](N)C(=O)O)c1)C(=O)O
|
| ZINC1834295 | 0.793 | 252.3 Da LogP -0.40 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O
|
| ZINC1834297 | 0.793 | 252.3 Da LogP -0.40 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O
|
| ZINC113264413 | 0.778 | 317.4 Da LogP 3.98 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O
|
| ZINC113264415 | 0.778 | 317.4 Da LogP 3.98 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O
|
| ZINC2244337 | 0.778 | 241.3 Da LogP 2.31 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O
|
| ZINC2244338 | 0.778 | 241.3 Da LogP 2.31 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O
|
| ZINC2512061 | 0.774 | 360.4 Da LogP 0.67 TPSA 167.1 | 1 viol. | ✓ Clean |
N[C@@H](Cc1ccc(O)c(-c2cc(C[C@H](N)C(=O)O)ccc2O)…
|
| ZINC53188912 | 0.753 | 485.5 Da LogP -0.45 TPSA 152.1 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N(C)[C@@H]2[C@H](CO)O[C@…
|
| ZINC53188914 | 0.753 | 485.5 Da LogP -0.45 TPSA 152.1 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N(C)[C@@H]2[C@H](CO)O[C@…
|
| ZINC53188917 | 0.753 | 485.5 Da LogP -0.45 TPSA 152.1 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N(C)[C@H]2[C@H](O)[C@@H]…
|
| ZINC53188920 | 0.753 | 485.5 Da LogP -0.45 TPSA 152.1 | 1 viol. | ✓ Clean |
COc1ccc(C[C@@H](N)C(=O)N(C)[C@H]2[C@H](O)[C@H](…
|
| ZINC39351856 | 0.741 | 328.4 Da LogP 1.26 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…
|
| ZINC2561081 | 0.724 | 269.3 Da LogP 1.87 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
N[C@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O
|
| ZINC2561082 | 0.724 | 269.3 Da LogP 1.87 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O
|
| ZINC113539705 | 0.700 | 265.3 Da LogP 2.04 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1ccc(C#Cc2ccccc2)cc1)C(=O)O
|
| ZINC113539708 | 0.700 | 265.3 Da LogP 2.04 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@H](Cc1ccc(C#Cc2ccccc2)cc1)C(=O)O
|
| ZINC116910786 | 0.700 | 269.3 Da LogP 3.06 TPSA 88.0 | ✓ Ro5 | Alert |
N[C@@H](Cc1ccc(/N=N/c2ccccc2)cc1)C(=O)O
|
| ZINC29566843 | 0.700 | 241.3 Da LogP 2.31 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@H](Cc1cccc(-c2ccccc2)c1)C(=O)O
|
| ZINC29570997 | 0.700 | 241.3 Da LogP 2.31 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1cccc(-c2ccccc2)c1)C(=O)O
|
| ZINC44283581 | 0.700 | 257.3 Da LogP 2.43 TPSA 72.5 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1ccc(Oc2ccccc2)cc1)C(=O)O
|
| ZINC44283583 | 0.700 | 257.3 Da LogP 2.43 TPSA 72.5 | ✓ Ro5 | ✓ Clean |
N[C@H](Cc1ccc(Oc2ccccc2)cc1)C(=O)O
|
| ZINC2111574 | 0.692 | 252.3 Da LogP -0.40 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1ccccc1C[C@H](N)C(=O)O)C(=O)O
|
| ZINC2111575 | 0.692 | 252.3 Da LogP -0.40 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@@H](Cc1ccccc1C[C@@H](N)C(=O)O)C(=O)O
|
| ZINC2111578 | 0.692 | 252.3 Da LogP -0.40 TPSA 126.6 | ✓ Ro5 | ✓ Clean |
N[C@H](Cc1ccccc1C[C@@H](N)C(=O)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.