Reaction Details |
| Report a problem with these data |
Target | Glutamate carboxypeptidase 2 |
---|
Ligand | BDBM50610873 |
---|
Substrate/Competitor | n/a |
---|
Meas. Tech. | ChEMBL_2282296 |
---|
IC50 | 7.1±n/a nM |
---|
Citation | Petrov, SA; Zyk, NY; Machulkin, AE; Beloglazkina, EK; Majouga, AG PSMA-targeted low-molecular double conjugates for diagnostics and therapy. Eur J Med Chem225:0 (2021) [PubMed] |
---|
More Info.: | Get all data from this article, Assay Method |
---|
|
Glutamate carboxypeptidase 2 |
---|
Name: | Glutamate carboxypeptidase 2 |
Synonyms: | FGCP | FOLH | FOLH1 | FOLH1_HUMAN | Folate hydrolase 1 | Folylpoly-gamma-glutamate carboxypeptidase | Glutamate carboxypeptidase 2 | Glutamate carboxypeptidase II | Membrane glutamate carboxypeptidase | N-acetylated-alpha-linked acidic dipeptidase I | NAALAD1 | NAALADase I | PSM | PSMA | Prostate-specific membrane antigen | Pteroylpoly-gamma-glutamate carboxypeptidase | mGCP |
Type: | PROTEIN |
Mol. Mass.: | 84333.66 |
Organism: | Homo sapiens (Human) |
Description: | ChEMBL_1497035 |
Residue: | 750 |
Sequence: | MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKA
FLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYP
NKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYA
RTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVK
SYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYY
DAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIG
TLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFAS
WDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKE
LKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKN
WETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDY
AVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIV
LRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVD
PSKAWGEVKRQIYVAAFTVQAAAETLSEVA
|
|
|
BDBM50610873 |
---|
n/a |
---|
Name | BDBM50610873 |
Synonyms: | CHEMBL5277672 |
Type | Small organic molecule |
Emp. Form. | C62H96FN11O26Si |
Mol. Mass. | 1458.5676 |
SMILES | [#6]C([#6])([#6])[Si;v4](F)(c1ccc(cc1)-[#6](=O)-[#7]-[#6]-[#6@@H](-[#7]-[#6](=O)-[#6]-[#6](-[#7]-1-[#6]-[#6]-[#7](-[#6]-[#6](-[#8])=O)-[#6]-[#6]-[#7](-[#6]-[#6](-[#8])=O)-[#6]-[#6]-[#7](-[#6]-[#6](-[#8])=O)-[#6]-[#6]-1)-[#6](-[#8])=O)-[#6](=O)-[#7]-[#6@H](-[#6]-[#6]-[#6]-[#6]-[#7]-[#6](=O)-[#6]-[#6]-[#6](=O)-[#7]-[#6]-[#6]-[#6]-[#6@@H](-[#7]-[#6](=O)-[#6]-[#6]-[#6@H](-[#7]-[#6](=O)-[#8]-[#6@@H](-[#6]-[#6]-[#6](-[#8])=O)-[#6](-[#8])=O)-[#6](-[#8])=O)-[#6](-[#8])=O)-[#6](-[#8])=O)C([#6])([#6])[#6] |r| |
Structure |
|