4M30
Crystal structure of RNASE III complexed with double-stranded RNA AND AMP (TYPE II CLEAVAGE)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003725 | molecular_function | double-stranded RNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004525 | molecular_function | ribonuclease III activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006364 | biological_process | rRNA processing |
| A | 0006396 | biological_process | RNA processing |
| A | 0006397 | biological_process | mRNA processing |
| A | 0008033 | biological_process | tRNA processing |
| A | 0010468 | biological_process | regulation of gene expression |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003725 | molecular_function | double-stranded RNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004525 | molecular_function | ribonuclease III activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006364 | biological_process | rRNA processing |
| B | 0006396 | biological_process | RNA processing |
| B | 0006397 | biological_process | mRNA processing |
| B | 0008033 | biological_process | tRNA processing |
| B | 0010468 | biological_process | regulation of gene expression |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | ASP44 |
| A | GLU110 |
| A | MG502 |
| A | HOH601 |
| C | AMP103 |
| D | U28 |
| D | HOH201 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | MG501 |
| A | HOH602 |
| A | HOH603 |
| C | AMP103 |
| A | GLU40 |
| A | GLU110 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 301 |
| Chain | Residue |
| B | ASP44 |
| B | GLU110 |
| B | MG302 |
| B | HOH401 |
| C | U28 |
| C | HOH218 |
| D | AMP104 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | GLU40 |
| B | GLU110 |
| B | MG301 |
| B | HOH414 |
| D | AMP104 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 303 |
| Chain | Residue |
| A | ILE118 |
| B | VAL56 |
| B | GLN57 |
| B | LYS62 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 101 |
| Chain | Residue |
| A | HOH621 |
| A | HOH622 |
| A | HOH623 |
| C | A2 |
| C | HOH215 |
| C | HOH216 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 102 |
| Chain | Residue |
| C | A2 |
| C | A3 |
| C | HOH213 |
| C | HOH214 |
| C | HOH217 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AMP C 103 |
| Chain | Residue |
| A | GLU40 |
| A | PHE41 |
| A | ASP44 |
| A | GLU110 |
| A | MG501 |
| A | MG502 |
| A | HOH602 |
| A | HOH603 |
| A | HOH622 |
| B | SER68 |
| B | LYS71 |
| C | A2 |
| C | U26 |
| C | A27 |
| D | U28 |
| D | HOH201 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG D 101 |
| Chain | Residue |
| A | GLU64 |
| A | HOH624 |
| B | HOH415 |
| D | A2 |
| D | HOH209 |
| D | HOH211 |
| D | HOH212 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 102 |
| Chain | Residue |
| D | A2 |
| D | A3 |
| D | HOH204 |
| D | HOH210 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG D 103 |
| Chain | Residue |
| D | C23 |
| site_id | BC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AMP D 104 |
| Chain | Residue |
| A | GLU64 |
| A | SER68 |
| A | LYS71 |
| B | GLU40 |
| B | PHE41 |
| B | ASP44 |
| B | GLU110 |
| B | MG301 |
| B | MG302 |
| B | HOH414 |
| C | U28 |
| C | HOH218 |
| D | A2 |
| D | U26 |
| D | A27 |
| D | HOH211 |
Functional Information from PROSITE/UniProt
| site_id | PS00517 |
| Number of Residues | 9 |
| Details | RNASE_3_1 Ribonuclease III family signature. ETLEFLGDA |
| Chain | Residue | Details |
| A | GLU37-ALA45 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 234 |
| Details | Domain: {"description":"RNase III"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 136 |
| Details | Domain: {"description":"DRBM"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15016361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18047582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11738048","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1JFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RC5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
