3ORZ
PDK1 mutant bound to allosteric disulfide fragment activator 2A2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 2A2 A 1 |
| Chain | Residue |
| A | LYS115 |
| A | ILE118 |
| A | ILE119 |
| A | ILE119 |
| A | CYS148 |
| A | PHE149 |
| A | LEU155 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BI4 A 360 |
| Chain | Residue |
| A | GLY91 |
| A | ALA109 |
| A | LYS111 |
| A | VAL143 |
| A | LEU159 |
| A | SER160 |
| A | TYR161 |
| A | ALA162 |
| A | GLU209 |
| A | LEU212 |
| A | THR222 |
| A | ASP223 |
| A | HOH393 |
| A | LEU88 |
| A | GLY89 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 2A2 B 1 |
| Chain | Residue |
| B | LYS115 |
| B | ILE118 |
| B | ILE119 |
| B | ARG131 |
| B | CYS148 |
| B | PHE149 |
| B | LEU155 |
| D | 2A21 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BI4 B 360 |
| Chain | Residue |
| B | LEU88 |
| B | GLY89 |
| B | GLU90 |
| B | GLY91 |
| B | ALA109 |
| B | LYS111 |
| B | VAL143 |
| B | LEU159 |
| B | SER160 |
| B | TYR161 |
| B | ALA162 |
| B | GLU209 |
| B | LEU212 |
| B | THR222 |
| B | ASP223 |
| B | HOH375 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 2A2 C 1 |
| Chain | Residue |
| C | LYS115 |
| C | ILE118 |
| C | ILE119 |
| C | CYS148 |
| C | PHE149 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BI4 C 360 |
| Chain | Residue |
| C | LEU88 |
| C | GLY89 |
| C | GLY91 |
| C | ALA109 |
| C | LYS111 |
| C | VAL143 |
| C | LEU159 |
| C | SER160 |
| C | TYR161 |
| C | ALA162 |
| C | GLU209 |
| C | LEU212 |
| C | THR222 |
| C | ASP223 |
| C | HOH373 |
| C | HOH823 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 2A2 D 1 |
| Chain | Residue |
| B | 2A21 |
| D | LYS115 |
| D | ILE118 |
| D | VAL124 |
| D | ARG131 |
| D | CYS148 |
| D | PHE149 |
| D | LEU155 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BI4 D 360 |
| Chain | Residue |
| D | LEU88 |
| D | GLY89 |
| D | GLY91 |
| D | ALA109 |
| D | LYS111 |
| D | VAL143 |
| D | LEU159 |
| D | SER160 |
| D | TYR161 |
| D | ALA162 |
| D | GLU209 |
| D | LEU212 |
| D | THR222 |
| D | ASP223 |
| D | HOH378 |
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 | 176 |
| Details | Region: {"description":"PIF-pocket","evidences":[{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 | 28 |
| 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 | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| 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 | 4 |
| 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 | 4 |
| Details | Modified residue: {"description":"Phosphothreonine; by MELK","evidences":[{"source":"PubMed","id":"22544756","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
