2BZJ
CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH A RUTHENIUM ORGANOMETALLIC LIGAND RU3
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 | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007346 | biological_process | regulation of mitotic cell cycle |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0045824 | biological_process | negative regulation of innate immune response |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0050821 | biological_process | protein stabilization |
| A | 0060045 | biological_process | positive regulation of cardiac muscle cell proliferation |
| A | 0070561 | biological_process | vitamin D receptor signaling pathway |
| A | 0071346 | biological_process | cellular response to type II interferon |
| A | 0090336 | biological_process | positive regulation of brown fat cell differentiation |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1900425 | biological_process | negative regulation of defense response to bacterium |
| A | 1902033 | biological_process | regulation of hematopoietic stem cell proliferation |
| A | 1904263 | biological_process | positive regulation of TORC1 signaling |
| A | 1905062 | biological_process | positive regulation of cardioblast proliferation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ME3 A1306 |
| Chain | Residue |
| A | LEU44 |
| A | GLU121 |
| A | ARG122 |
| A | PRO123 |
| A | ASP128 |
| A | GLU171 |
| A | LEU174 |
| A | ILE185 |
| A | ASP186 |
| A | HOH2140 |
| A | GLY45 |
| A | PHE49 |
| A | VAL52 |
| A | ALA65 |
| A | LYS67 |
| A | GLU89 |
| A | ILE104 |
| A | LEU120 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK |
| Chain | Residue | Details |
| A | LEU44-LYS67 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI |
| Chain | Residue | Details |
| A | VAL163-ILE175 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 252 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| 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 | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15525646","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15657054","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15808862","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15657054","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP167 | |
| A | GLU171 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS169 | |
| A | ASP167 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR204 | |
| A | LYS169 | |
| A | ASP167 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN172 | |
| A | LYS169 | |
| A | ASP167 |
