2BZI
CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH A RUTHENIUM ORGANOMETALLIC LIGAND RU2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005730 | cellular_component | nucleolus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0006915 | biological_process | apoptotic process |
| B | 0007346 | biological_process | regulation of mitotic cell cycle |
| B | 0008134 | molecular_function | transcription factor binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0022898 | biological_process | regulation of transmembrane transporter activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0031669 | biological_process | cellular response to nutrient levels |
| B | 0034198 | biological_process | cellular response to amino acid starvation |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0043024 | molecular_function | ribosomal small subunit binding |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0043433 | biological_process | negative regulation of DNA-binding transcription factor activity |
| B | 0045824 | biological_process | negative regulation of innate immune response |
| B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| B | 0046777 | biological_process | protein autophosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050821 | biological_process | protein stabilization |
| B | 0051715 | biological_process | cytolysis in another organism |
| B | 0060045 | biological_process | positive regulation of cardiac muscle cell proliferation |
| B | 0070561 | biological_process | vitamin D receptor signaling pathway |
| B | 0071346 | biological_process | cellular response to type II interferon |
| B | 0090336 | biological_process | positive regulation of brown fat cell differentiation |
| B | 0106310 | molecular_function | protein serine kinase activity |
| B | 0160075 | biological_process | non-canonical inflammasome complex assembly |
| B | 1902033 | biological_process | regulation of hematopoietic stem cell proliferation |
| B | 1904262 | biological_process | negative regulation of TORC1 signaling |
| B | 1904263 | biological_process | positive regulation of TORC1 signaling |
| B | 1905062 | biological_process | positive regulation of cardioblast proliferation |
| B | 1990748 | biological_process | cellular detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE DW2 B1306 |
| Chain | Residue |
| B | LEU44 |
| B | GLU121 |
| B | ARG122 |
| B | ASP128 |
| B | GLU171 |
| B | LEU174 |
| B | ILE185 |
| B | ASP186 |
| B | HOH2049 |
| B | HOH2268 |
| B | GLY45 |
| B | PHE49 |
| B | VAL52 |
| B | ALA65 |
| B | LYS67 |
| B | GLU89 |
| B | ILE104 |
| B | 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 |
| B | LEU44-LYS67 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI |
| Chain | Residue | Details |
| B | VAL163-ILE175 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| B | ASP167 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| B | LEU44 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 |
| Chain | Residue | Details |
| B | LYS67 | |
| B | GLU121 | |
| B | ASP128 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| B | SER8 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15657054 |
| Chain | Residue | Details |
| B | THR23 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054 |
| Chain | Residue | Details |
| B | SER98 | |
| B | SEP261 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP167 | |
| B | GLU171 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS169 | |
| B | ASP167 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR204 | |
| B | LYS169 | |
| B | ASP167 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN172 | |
| B | LYS169 | |
| B | ASP167 |
