1Y44
Crystal structure of RNase Z
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0008033 | biological_process | tRNA processing |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016891 | molecular_function | RNA endonuclease activity producing 5'-phosphomonoesters, hydrolytic mechanism |
| A | 0042780 | biological_process | tRNA 3'-end processing |
| A | 0042781 | molecular_function | 3'-tRNA processing endoribonuclease activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0008033 | biological_process | tRNA processing |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016891 | molecular_function | RNA endonuclease activity producing 5'-phosphomonoesters, hydrolytic mechanism |
| B | 0042780 | biological_process | tRNA 3'-end processing |
| B | 0042781 | molecular_function | 3'-tRNA processing endoribonuclease 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 ZN A 400 |
| Chain | Residue |
| A | HIS63 |
| A | HIS65 |
| A | HIS140 |
| A | ASP211 |
| A | ZN401 |
| A | PO4945 |
| A | HOH1007 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | ASP211 |
| A | HIS269 |
| A | ZN400 |
| A | PO4945 |
| A | HOH1007 |
| A | ASP67 |
| A | HIS68 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 945 |
| Chain | Residue |
| A | GLY11 |
| A | HIS65 |
| A | ASP67 |
| A | HIS140 |
| A | ASP211 |
| A | HIS247 |
| A | HIS269 |
| A | ZN400 |
| A | ZN401 |
| A | HOH948 |
| A | HOH1007 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES B 801 |
| Chain | Residue |
| B | ARG31 |
| B | ARG54 |
| B | LYS55 |
| B | GLU57 |
| B | ASP86 |
| B | HOH859 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 601 |
| Chain | Residue |
| B | LYS176 |
| B | VAL183 |
| B | THR184 |
| B | PRO291 |
| B | ASN292 |
| B | HOH861 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 602 |
| Chain | Residue |
| A | HIS48 |
| A | PHE299 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 603 |
| Chain | Residue |
| A | ARG31 |
| A | ARG54 |
| A | LYS55 |
| A | ILE56 |
| A | GLU57 |
| A | ARG79 |
| A | ASP86 |
| A | GLU87 |
| A | HOH983 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01818","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15654328","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01818","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15654328","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01818","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15654328","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16518398","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
