5LVL
Human PDK1 Kinase Domain in Complex with Compound PS653 Bound to the ATP-Binding Site
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue 537 A 401 |
| Chain | Residue |
| A | LEU88 |
| A | ALA109 |
| A | LEU159 |
| A | SER160 |
| A | TYR161 |
| A | ALA162 |
| A | GLY165 |
| A | LEU212 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue DTD A 402 |
| Chain | Residue |
| A | VAL243 |
| A | GLY244 |
| A | THR245 |
| A | ALA246 |
| A | GLU287 |
| A | PHE291 |
| A | HOH629 |
| A | PHE242 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue DMS A 403 |
| Chain | Residue |
| A | THR104 |
| A | SER105 |
| A | HIS139 |
| A | PHE141 |
| A | SER191 |
| A | TRP347 |
| A | GLU348 |
| A | ASN349 |
| A | LEU350 |
| A | HIS351 |
| A | HOH542 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 404 |
| Chain | Residue |
| A | PHE84 |
| A | ILE112 |
| A | LYS154 |
| A | TYR156 |
| A | GLU331 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 405 |
| Chain | Residue |
| A | TYR299 |
| A | ASP300 |
| A | PHE301 |
| A | GLU314 |
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 |
