2OI4
Crystal structure of human PIM1 in complex with fluorinated ruthenium pyridocarbazole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| X | 0000166 | molecular_function | nucleotide binding |
| X | 0004672 | molecular_function | protein kinase activity |
| X | 0004674 | molecular_function | protein serine/threonine kinase activity |
| X | 0005515 | molecular_function | protein binding |
| X | 0005524 | molecular_function | ATP binding |
| X | 0005634 | cellular_component | nucleus |
| X | 0005654 | cellular_component | nucleoplasm |
| X | 0005730 | cellular_component | nucleolus |
| X | 0005737 | cellular_component | cytoplasm |
| X | 0005829 | cellular_component | cytosol |
| X | 0005886 | cellular_component | plasma membrane |
| X | 0006468 | biological_process | protein phosphorylation |
| X | 0006915 | biological_process | apoptotic process |
| X | 0007346 | biological_process | regulation of mitotic cell cycle |
| X | 0016301 | molecular_function | kinase activity |
| X | 0016740 | molecular_function | transferase activity |
| X | 0030145 | molecular_function | manganese ion binding |
| X | 0043066 | biological_process | negative regulation of apoptotic process |
| X | 0045824 | biological_process | negative regulation of innate immune response |
| X | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| X | 0046872 | molecular_function | metal ion binding |
| X | 0050821 | biological_process | protein stabilization |
| X | 0060045 | biological_process | positive regulation of cardiac muscle cell proliferation |
| X | 0070561 | biological_process | vitamin D receptor signaling pathway |
| X | 0071346 | biological_process | cellular response to type II interferon |
| X | 0090336 | biological_process | positive regulation of brown fat cell differentiation |
| X | 0106310 | molecular_function | protein serine kinase activity |
| X | 1902033 | biological_process | regulation of hematopoietic stem cell proliferation |
| X | 1904263 | biological_process | positive regulation of TORC1 signaling |
| X | 1905062 | biological_process | positive regulation of cardioblast proliferation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL X 1001 |
| Chain | Residue |
| X | VAL69 |
| X | GLU70 |
| X | ARG73 |
| X | THR196 |
| X | EDO1002 |
| X | HOH2794 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE JM1 X 1000 |
| Chain | Residue |
| X | VAL52 |
| X | ALA65 |
| X | LYS67 |
| X | ILE104 |
| X | LEU120 |
| X | GLU121 |
| X | ARG122 |
| X | PRO123 |
| X | GLU171 |
| X | LEU174 |
| X | ILE185 |
| X | ASP186 |
| X | LEU44 |
| X | GLY45 |
| X | PHE49 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO X 1002 |
| Chain | Residue |
| X | GLY47 |
| X | GLY48 |
| X | VAL69 |
| X | ARG73 |
| X | CL1001 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO X 1003 |
| Chain | Residue |
| X | LEU34 |
| X | GLU35 |
| X | VAL40 |
| X | ILE66 |
| X | HIS68 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO X 1004 |
| Chain | Residue |
| X | GLN257 |
| X | ARG258 |
| X | ASN286 |
| X | HOH2850 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE EPE X 2691 |
| Chain | Residue |
| X | GLY48 |
| X | PHE49 |
| X | LYS67 |
| X | VAL69 |
| X | PRO87 |
| X | GLU89 |
| X | ASP167 |
| X | ASP186 |
| X | GLY188 |
| X | SER189 |
| X | ASP202 |
| X | HOH2709 |
| X | HOH2807 |
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 |
| X | LEU44-LYS67 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI |
| Chain | Residue | Details |
| X | 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 |
| X | ASP167 | |
| X | GLU171 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| X | LYS169 | |
| X | ASP167 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| X | THR204 | |
| X | LYS169 | |
| X | ASP167 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| X | ASN172 | |
| X | LYS169 | |
| X | ASP167 |
