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6IEH

Crystal structures of the hMTR4-NRDE2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0000176cellular_componentnuclear exosome (RNase complex)
B0000178cellular_componentexosome (RNase complex)
B0000398biological_processmRNA splicing, via spliceosome
B0000460biological_processmaturation of 5.8S rRNA
B0003676molecular_functionnucleic acid binding
B0003689molecular_functionDNA clamp loader activity
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
B0006338biological_processchromatin remodeling
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
B0061775molecular_functioncohesin loader activity
B0071013cellular_componentcatalytic step 2 spliceosome
B0140584molecular_functionchromatin extrusion motor activity
B0140588biological_processchromatin looping
B0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
B0140849molecular_functionATP-dependent H2AZ histone chaperone activity
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 Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:31358741, ECO:0007744|PDB:6RO1
ChainResidueDetails
BILE139

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
BALA161

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:29844170, ECO:0000269|PubMed:31358741, ECO:0007744|PDB:6C90, ECO:0007744|PDB:6RO1
ChainResidueDetails
BSER164
BGLY166
BLYS167
BTHR168

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CZU3
ChainResidueDetails
BLYS78

site_idSWS_FT_FI5
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS358
BLYS723

site_idSWS_FT_FI6
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS684

227111

PDB entries from 2024-11-06

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