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6IEH

Crystal structures of the hMTR4-NRDE2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0000176cellular_componentnuclear exosome (RNase complex)
B0000178cellular_componentexosome (RNase complex)
B0000398biological_processmRNA splicing, via spliceosome
B0000460biological_processmaturation of 5.8S rRNA
B0003676molecular_functionnucleic acid binding
B0003723molecular_functionRNA binding
B0003724molecular_functionRNA helicase activity
B0004386molecular_functionhelicase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005681cellular_componentspliceosomal complex
B0005730cellular_componentnucleolus
B0006364biological_processrRNA processing
B0006397biological_processmRNA processing
B0006401biological_processRNA catabolic process
B0006974biological_processDNA damage response
B0008380biological_processRNA splicing
B0016076biological_processsnRNA catabolic process
B0016607cellular_componentnuclear speck
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0031499cellular_componentTRAMP complex
B0071013cellular_componentcatalytic step 2 spliceosome
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL B 1101
ChainResidue
BMET726
BLEU750
BARG756

site_idAC2
Number of Residues12
Detailsbinding site for residue ATP B 1102
ChainResidue
BLYS167
BTHR168
BLYS198
BASP252
BGLU253
BARG527
BPHE138
BILE139
BGLN144
BTHR163
BSER164
BGLY166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues156
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues172
DetailsDomain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsMotif: {"description":"DEIH box"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31358741","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6RO1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsCross-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"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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