4OAV
Complete human RNase L in complex with 2-5A (5'-ppp heptamer), AMPPCP and RNA substrate.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004521 | molecular_function | RNA endonuclease activity |
| B | 0004540 | molecular_function | RNA nuclease activity |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006364 | biological_process | rRNA processing |
| B | 0006396 | biological_process | RNA processing |
| B | 0006397 | biological_process | mRNA processing |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0010468 | biological_process | regulation of gene expression |
| B | 0016363 | cellular_component | nuclear matrix |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019843 | molecular_function | rRNA binding |
| B | 0043021 | molecular_function | ribonucleoprotein complex binding |
| B | 0043488 | biological_process | regulation of mRNA stability |
| B | 0045071 | biological_process | negative regulation of viral genome replication |
| B | 0045444 | biological_process | fat cell differentiation |
| B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| B | 0046326 | biological_process | positive regulation of D-glucose import |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051252 | biological_process | regulation of RNA metabolic process |
| B | 0051607 | biological_process | defense response to virus |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003723 | molecular_function | RNA binding |
| D | 0004518 | molecular_function | nuclease activity |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0004521 | molecular_function | RNA endonuclease activity |
| D | 0004540 | molecular_function | RNA nuclease activity |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0005829 | cellular_component | cytosol |
| D | 0006364 | biological_process | rRNA processing |
| D | 0006396 | biological_process | RNA processing |
| D | 0006397 | biological_process | mRNA processing |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0010468 | biological_process | regulation of gene expression |
| D | 0016363 | cellular_component | nuclear matrix |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019843 | molecular_function | rRNA binding |
| D | 0043021 | molecular_function | ribonucleoprotein complex binding |
| D | 0043488 | biological_process | regulation of mRNA stability |
| D | 0045071 | biological_process | negative regulation of viral genome replication |
| D | 0045444 | biological_process | fat cell differentiation |
| D | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| D | 0046326 | biological_process | positive regulation of D-glucose import |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051252 | biological_process | regulation of RNA metabolic process |
| D | 0051607 | biological_process | defense response to virus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ACP B 801 |
| Chain | Residue |
| B | ILE371 |
| B | THR435 |
| B | CYS437 |
| B | THR440 |
| B | GLN489 |
| B | ASN490 |
| B | LEU492 |
| B | ASP503 |
| B | ASP505 |
| B | MG802 |
| B | MG803 |
| B | ALA372 |
| B | HOH907 |
| B | HOH918 |
| B | HOH926 |
| B | HOH955 |
| B | HOH989 |
| B | HOH1072 |
| B | THR374 |
| B | SER375 |
| B | ILE379 |
| B | ALA390 |
| B | LYS392 |
| B | ARG400 |
| B | VAL434 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 802 |
| Chain | Residue |
| B | ASN490 |
| B | ASP503 |
| B | ACP801 |
| B | HOH907 |
| B | HOH918 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 803 |
| Chain | Residue |
| B | ASP485 |
| B | ASP503 |
| B | ASP505 |
| B | ACP801 |
| B | HOH926 |
| B | HOH1143 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ACP D 1001 |
| Chain | Residue |
| D | ILE371 |
| D | ALA372 |
| D | THR374 |
| D | SER375 |
| D | ILE379 |
| D | ALA390 |
| D | LYS392 |
| D | ARG400 |
| D | VAL434 |
| D | THR435 |
| D | CYS437 |
| D | THR440 |
| D | GLN489 |
| D | ASN490 |
| D | LEU492 |
| D | ASP503 |
| D | ASP505 |
| D | MG1002 |
| D | MG1003 |
| D | HOH1122 |
| D | HOH1147 |
| D | HOH1191 |
| D | HOH1196 |
| D | HOH1242 |
| D | HOH1281 |
| D | HOH1318 |
| D | HOH1402 |
| D | HOH1468 |
| D | HOH1492 |
| D | HOH1493 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1002 |
| Chain | Residue |
| D | ASN490 |
| D | ASP503 |
| D | ACP1001 |
| D | HOH1122 |
| D | HOH1492 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1003 |
| Chain | Residue |
| D | ASP503 |
| D | ASP505 |
| D | ACP1001 |
| D | HOH1493 |
| D | HOH1494 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PUP D 1004 |
| Chain | Residue |
| D | LYS606 |
| D | THR607 |
| D | MET644 |
| D | PHE647 |
| D | TYR648 |
| D | ARG651 |
| D | ARG667 |
| D | ASN668 |
| D | ASN672 |
| D | HOH1128 |
| D | HOH1270 |
| D | HOH1350 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 29 |
| Details | Repeat: {"description":"ANK 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 58 |
| Details | Repeat: {"description":"ANK 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 58 |
| Details | Repeat: {"description":"ANK 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 58 |
| Details | Repeat: {"description":"ANK 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 60 |
| Details | Repeat: {"description":"ANK 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"ANK 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 60 |
| Details | Repeat: {"description":"ANK 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 58 |
| Details | Repeat: {"description":"ANK 8"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 98 |
| Details | Zinc finger: {"description":"C6-type; atypical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 26 |
| Details | Region: {"description":"2-5A binding (P-loop) 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 44 |
| Details | Region: {"description":"2-5A binding (P-loop) 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
