4O1P
Crystal Structure of RNase L in complex with 2-5A and AMP-PNP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004540 | molecular_function | RNA nuclease activity |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006396 | biological_process | RNA processing |
| A | 0006397 | biological_process | mRNA processing |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0045071 | biological_process | negative regulation of viral genome replication |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051252 | biological_process | regulation of RNA metabolic process |
| A | 0051607 | biological_process | defense response to virus |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004540 | molecular_function | RNA nuclease activity |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006396 | biological_process | RNA processing |
| B | 0006397 | biological_process | mRNA processing |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0045071 | biological_process | negative regulation of viral genome replication |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051252 | biological_process | regulation of RNA metabolic process |
| B | 0051607 | biological_process | defense response to virus |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0004540 | molecular_function | RNA nuclease activity |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006396 | biological_process | RNA processing |
| C | 0006397 | biological_process | mRNA processing |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0045071 | biological_process | negative regulation of viral genome replication |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051252 | biological_process | regulation of RNA metabolic process |
| C | 0051607 | biological_process | defense response to virus |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003723 | molecular_function | RNA binding |
| D | 0004540 | molecular_function | RNA nuclease activity |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006396 | biological_process | RNA processing |
| D | 0006397 | biological_process | mRNA processing |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0045071 | biological_process | negative regulation of viral genome replication |
| 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 | 18 |
| Details | BINDING SITE FOR RESIDUE ANP A 901 |
| Chain | Residue |
| A | ALA370 |
| A | GLN486 |
| A | ASN487 |
| A | LEU489 |
| A | ASP500 |
| A | ASP502 |
| A | MG902 |
| A | MG903 |
| A | HOH1046 |
| A | HOH1084 |
| A | THR372 |
| A | ALA373 |
| A | ILE377 |
| A | ALA388 |
| A | LYS390 |
| A | ALA433 |
| A | CYS435 |
| A | THR438 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 902 |
| Chain | Residue |
| A | ASP500 |
| A | ASP502 |
| A | ANP901 |
| A | MG903 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 903 |
| Chain | Residue |
| A | ASN487 |
| A | ASP500 |
| A | ANP901 |
| A | MG902 |
| A | HOH1046 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE 25L A 904 |
| Chain | Residue |
| A | TRP56 |
| A | TRP58 |
| A | SER63 |
| A | GLN66 |
| A | LYS87 |
| A | ASN89 |
| A | ILE99 |
| A | ASN122 |
| A | PHE124 |
| A | GLU129 |
| A | TYR133 |
| A | ARG153 |
| A | LYS164 |
| A | HOH1002 |
| A | HOH1020 |
| A | HOH1024 |
| A | HOH1028 |
| A | HOH1035 |
| A | HOH1052 |
| A | HOH1064 |
| A | HOH1112 |
| A | HOH1222 |
| B | ARG307 |
| B | ARG308 |
| B | TYR310 |
| B | ARG353 |
| B | PHE362 |
| B | HOH1089 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ANP B 901 |
| Chain | Residue |
| B | ALA370 |
| B | THR372 |
| B | ALA373 |
| B | ILE377 |
| B | ALA388 |
| B | LYS390 |
| B | ALA433 |
| B | CYS435 |
| B | THR438 |
| B | GLN486 |
| B | ASN487 |
| B | LEU489 |
| B | ASP500 |
| B | ASP502 |
| B | MG902 |
| B | MG903 |
| B | HOH1023 |
| B | HOH1076 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 902 |
| Chain | Residue |
| B | ARG398 |
| B | ASP500 |
| B | ASP502 |
| B | ANP901 |
| B | MG903 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 903 |
| Chain | Residue |
| B | ASN487 |
| B | ASP500 |
| B | ANP901 |
| B | MG902 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE 25L B 904 |
| Chain | Residue |
| B | GLU129 |
| B | TYR133 |
| B | ARG153 |
| B | LYS164 |
| B | HOH1003 |
| B | HOH1012 |
| B | HOH1102 |
| B | HOH1122 |
| B | HOH1140 |
| B | HOH1165 |
| B | HOH1233 |
| A | ARG307 |
| A | ARG308 |
| A | TYR310 |
| A | ARG353 |
| A | PHE362 |
| A | HOH1071 |
| A | HOH1110 |
| B | TRP56 |
| B | TRP58 |
| B | SER63 |
| B | GLN66 |
| B | LYS87 |
| B | ASN89 |
| B | ILE99 |
| B | ASP120 |
| B | ASN122 |
| B | PHE124 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ANP C 901 |
| Chain | Residue |
| C | ALA370 |
| C | THR372 |
| C | ALA373 |
| C | ILE377 |
| C | ALA388 |
| C | LYS390 |
| C | ALA433 |
| C | CYS435 |
| C | THR438 |
| C | GLN486 |
| C | ASN487 |
| C | LEU489 |
| C | ASP500 |
| C | ASP502 |
| C | MG902 |
| C | MG903 |
| C | HOH1011 |
| C | HOH1023 |
| C | HOH1056 |
| C | HOH1072 |
| C | HOH1194 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 902 |
| Chain | Residue |
| C | ASP500 |
| C | ASP502 |
| C | ANP901 |
| C | MG903 |
| C | HOH1011 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 903 |
| Chain | Residue |
| C | ASN487 |
| C | ASP500 |
| C | ANP901 |
| C | MG902 |
| site_id | BC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE 25L C 904 |
| Chain | Residue |
| C | TRP56 |
| C | TRP58 |
| C | SER63 |
| C | GLN66 |
| C | LYS87 |
| C | ASN89 |
| C | ASP120 |
| C | ASN122 |
| C | PHE124 |
| C | GLU129 |
| C | TYR133 |
| C | ARG153 |
| C | LYS164 |
| C | HOH1003 |
| C | HOH1005 |
| C | HOH1007 |
| C | HOH1021 |
| C | HOH1048 |
| C | HOH1052 |
| C | HOH1059 |
| C | HOH1087 |
| C | HOH1100 |
| C | HOH1108 |
| C | HOH1148 |
| C | HOH1208 |
| C | HOH1216 |
| D | ARG307 |
| D | ARG308 |
| D | TYR310 |
| D | ARG353 |
| D | PHE362 |
| D | SER426 |
| D | HOH1012 |
| site_id | BC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ANP D 901 |
| Chain | Residue |
| D | ALA370 |
| D | THR372 |
| D | ALA373 |
| D | ILE377 |
| D | ALA388 |
| D | LYS390 |
| D | ARG398 |
| D | ALA433 |
| D | CYS435 |
| D | THR438 |
| D | GLN486 |
| D | ASN487 |
| D | LEU489 |
| D | ASP500 |
| D | ASP502 |
| D | MG902 |
| D | MG903 |
| D | HOH1132 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 902 |
| Chain | Residue |
| D | GLN486 |
| D | ASN487 |
| D | ASP500 |
| D | ANP901 |
| D | MG903 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 903 |
| Chain | Residue |
| D | ASP482 |
| D | ASN487 |
| D | ASP500 |
| D | ANP901 |
| D | MG902 |
| site_id | BC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE 25L D 904 |
| Chain | Residue |
| C | ARG307 |
| C | TYR310 |
| C | ARG353 |
| C | PHE362 |
| C | HOH1130 |
| D | TRP56 |
| D | TRP58 |
| D | SER63 |
| D | GLN66 |
| D | LYS87 |
| D | ASN89 |
| D | ASN122 |
| D | PHE124 |
| D | GLU129 |
| D | TYR133 |
| D | ARG153 |
| D | LYS164 |
| D | HOH1003 |
| D | HOH1041 |
| D | HOH1055 |
| D | HOH1155 |
| D | HOH1156 |
| D | HOH1189 |
| D | HOH1205 |
| D | HOH1232 |
Functional Information from PROSITE/UniProt
| site_id | PS00066 |
| Number of Residues | 15 |
| Details | HMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. KaEVdARDnMGrNaL |
| Chain | Residue | Details |
| A | LYS190-LEU204 |
