2NUG
Crystal structure of RNase III from Aquifex aeolicus complexed with ds-RNA at 1.7-Angstrom Resolution
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 | HOH518 |
| A | HOH519 |
| D | G12 |
| D | HOH517 |
| E | A17 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | MG503 |
| A | HOH519 |
| A | HOH520 |
| A | HOH531 |
| E | A17 |
| E | HOH506 |
| A | GLU40 |
| A | GLU110 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | ASP107 |
| A | MG502 |
| A | HOH521 |
| A | HOH522 |
| A | HOH523 |
| E | HOH506 |
| E | HOH507 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 504 |
| Chain | Residue |
| A | GLU37 |
| A | GLU40 |
| A | HOH524 |
| A | HOH525 |
| B | HOH519 |
| E | G18 |
| E | HOH508 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 505 |
| Chain | Residue |
| E | A17 |
| E | G18 |
| E | HOH509 |
| E | HOH510 |
| E | HOH511 |
| E | HOH512 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 506 |
| Chain | Residue |
| A | HOH526 |
| A | HOH527 |
| A | HOH528 |
| A | HOH529 |
| C | HOH520 |
| C | HOH521 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 507 |
| Chain | Residue |
| B | ASP44 |
| B | GLU110 |
| B | HOH520 |
| C | G12 |
| C | HOH522 |
| C | HOH523 |
| F | A17 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 508 |
| Chain | Residue |
| B | GLU40 |
| B | GLU110 |
| B | HOH521 |
| B | HOH530 |
| C | HOH523 |
| F | A17 |
| F | HOH514 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 509 |
| Chain | Residue |
| B | ASP107 |
| B | HOH521 |
| B | HOH522 |
| B | HOH523 |
| B | HOH524 |
| B | HOH530 |
| F | HOH515 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 510 |
| Chain | Residue |
| A | HOH530 |
| B | GLU37 |
| B | GLU40 |
| B | HOH525 |
| B | HOH526 |
| F | HOH516 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 511 |
| Chain | Residue |
| F | A17 |
| F | G18 |
| F | HOH517 |
| F | HOH518 |
| F | HOH519 |
| F | HOH520 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 512 |
| Chain | Residue |
| B | HOH527 |
| B | HOH528 |
| B | HOH529 |
| D | HOH518 |
| D | HOH519 |
| D | HOH563 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 513 |
| Chain | Residue |
| E | HOH522 |
| F | HOH542 |
| F | HOH543 |
| F | HOH544 |
| F | HOH545 |
| F | HOH552 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 514 |
| Chain | Residue |
| D | HOH529 |
| D | HOH533 |
| D | HOH550 |
| D | HOH551 |
| D | HOH552 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 515 |
| Chain | Residue |
| C | HOH535 |
| C | HOH538 |
| C | HOH559 |
| C | HOH563 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 516 |
| Chain | Residue |
| E | HOH513 |
| E | HOH526 |
| D | HOH522 |
| D | HOH531 |
| D | HOH535 |
| D | HOH562 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 517 |
| Chain | Residue |
| A | GLY12 |
| A | HOH534 |
| A | HOH620 |
| A | HOH632 |
| B | ARG194 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 518 |
| Chain | Residue |
| B | HOH538 |
| B | HOH561 |
| B | HOH657 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 519 |
| Chain | Residue |
| C | HOH526 |
| C | HOH530 |
| C | HOH540 |
| C | HOH546 |
| C | HOH562 |
| F | HOH551 |
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 | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 68 |
| Details | Domain: {"description":"DRBM"} |
| Chain | Residue | Details |






