6IEH
Crystal structures of the hMTR4-NRDE2 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000176 | cellular_component | nuclear exosome (RNase complex) |
B | 0000178 | cellular_component | exosome (RNase complex) |
B | 0000398 | biological_process | mRNA splicing, via spliceosome |
B | 0000460 | biological_process | maturation of 5.8S rRNA |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0003723 | molecular_function | RNA binding |
B | 0003724 | molecular_function | RNA helicase activity |
B | 0004386 | molecular_function | helicase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005681 | cellular_component | spliceosomal complex |
B | 0005730 | cellular_component | nucleolus |
B | 0006364 | biological_process | rRNA processing |
B | 0006397 | biological_process | mRNA processing |
B | 0006401 | biological_process | RNA catabolic process |
B | 0006974 | biological_process | DNA damage response |
B | 0008380 | biological_process | RNA splicing |
B | 0016076 | biological_process | snRNA catabolic process |
B | 0016607 | cellular_component | nuclear speck |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0031499 | cellular_component | TRAMP complex |
B | 0071013 | cellular_component | catalytic step 2 spliceosome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue CL B 1101 |
Chain | Residue |
B | MET726 |
B | LEU750 |
B | ARG756 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue ATP B 1102 |
Chain | Residue |
B | LYS167 |
B | THR168 |
B | LYS198 |
B | ASP252 |
B | GLU253 |
B | ARG527 |
B | PHE138 |
B | ILE139 |
B | GLN144 |
B | THR163 |
B | SER164 |
B | GLY166 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 156 |
Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 172 |
Details | Domain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Motif: {"description":"DEIH box"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"31358741","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6RO1","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"29844170","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31358741","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C90","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RO1","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |