3RWP
Discovery of a Novel, Potent and Selective Inhibitor of 3-Phosphoinositide Dependent Kinase (PDK1)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 901 |
| Chain | Residue |
| A | ARG106 |
| A | GLU107 |
| A | SER160 |
| A | TYR161 |
| A | HOH434 |
| A | SO4904 |
| A | SO4907 |
| A | SO4908 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 902 |
| Chain | Residue |
| A | THR104 |
| A | HIS139 |
| A | SER191 |
| A | TRP347 |
| A | GLU348 |
| A | ASN349 |
| A | LEU350 |
| A | HIS351 |
| A | ALA103 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 903 |
| Chain | Residue |
| A | PRO79 |
| A | PHE84 |
| A | LYS154 |
| A | TYR156 |
| A | GLU328 |
| A | GLU331 |
| A | GLY332 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 904 |
| Chain | Residue |
| A | ARG106 |
| A | HIS351 |
| A | HOH398 |
| A | HOH453 |
| A | GOL901 |
| A | SO4908 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 905 |
| Chain | Residue |
| A | LYS76 |
| A | ARG131 |
| A | THR148 |
| A | PHE149 |
| A | GLN150 |
| A | HOH386 |
| A | HOH414 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 906 |
| Chain | Residue |
| A | LYS144 |
| A | LYS144 |
| A | TYR146 |
| A | TYR146 |
| A | HOH453 |
| A | SO4907 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 907 |
| Chain | Residue |
| A | TYR146 |
| A | SER160 |
| A | GLN220 |
| A | HOH431 |
| A | HOH505 |
| A | GOL901 |
| A | SO4906 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 908 |
| Chain | Residue |
| A | ARG106 |
| A | GLU107 |
| A | HIS351 |
| A | GLN352 |
| A | HOH434 |
| A | GOL901 |
| A | SO4904 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 909 |
| Chain | Residue |
| A | GLN73 |
| A | ARG75 |
| A | ARG136 |
| A | LYS199 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 910 |
| Chain | Residue |
| A | HOH15 |
| A | GLY91 |
| A | SER92 |
| A | PHE93 |
| A | ABQ360 |
| A | HOH377 |
| A | HOH423 |
| A | HOH424 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ABQ A 360 |
| Chain | Residue |
| A | HOH1 |
| A | HOH3 |
| A | LEU88 |
| A | GLY89 |
| A | GLU90 |
| A | GLY91 |
| A | SER94 |
| A | THR95 |
| A | VAL96 |
| A | ALA109 |
| A | LYS111 |
| A | LEU159 |
| A | SER160 |
| A | ALA162 |
| A | GLU166 |
| A | GLU209 |
| A | LEU212 |
| A | THR222 |
| A | ASP223 |
| A | GOL910 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSFSTVVlArelatsre..........YAIK |
| Chain | Residue | Details |
| A | LEU88-LYS111 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNILL |
| Chain | Residue | Details |
| A | ILE201-LEU213 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | Region: {"description":"PIF-pocket","evidences":[{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12169624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15741170","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"10455013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11481331","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15772071","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16780920","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z2A0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by MELK","evidences":[{"source":"PubMed","id":"22544756","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
