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3KX2

Crystal structure of Prp43p in complex with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000390biological_processspliceosomal complex disassembly
A0000462biological_processmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0000463biological_processmaturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0000466biological_processmaturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0003724molecular_functionRNA helicase activity
A0003729molecular_functionmRNA binding
A0004386molecular_functionhelicase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005681cellular_componentspliceosomal complex
A0005739cellular_componentmitochondrion
A0006364biological_processrRNA processing
A0006397biological_processmRNA processing
A0008186molecular_functionATP-dependent activity, acting on RNA
A0008380biological_processRNA splicing
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0022613biological_processribonucleoprotein complex biogenesis
A0030490biological_processmaturation of SSU-rRNA
A0030686cellular_component90S preribosome
A0042273biological_processribosomal large subunit biogenesis
A0071014cellular_componentpost-mRNA release spliceosomal complex
B0000166molecular_functionnucleotide binding
B0000390biological_processspliceosomal complex disassembly
B0000462biological_processmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0000463biological_processmaturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0000466biological_processmaturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0003676molecular_functionnucleic acid binding
B0003723molecular_functionRNA binding
B0003724molecular_functionRNA helicase activity
B0003729molecular_functionmRNA binding
B0004386molecular_functionhelicase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005681cellular_componentspliceosomal complex
B0005739cellular_componentmitochondrion
B0006364biological_processrRNA processing
B0006397biological_processmRNA processing
B0008186molecular_functionATP-dependent activity, acting on RNA
B0008380biological_processRNA splicing
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0022613biological_processribonucleoprotein complex biogenesis
B0030490biological_processmaturation of SSU-rRNA
B0030686cellular_component90S preribosome
B0042273biological_processribosomal large subunit biogenesis
B0071014cellular_componentpost-mRNA release spliceosomal complex
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 800
ChainResidue
BTHR123
BSER382
BHOH901
BHOH902
BHOH903
BHOH904
BADP1000

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ADP B 1000
ChainResidue
BTHR118
BGLY119
BSER120
BGLY121
BLYS122
BTHR123
BTHR124
BARG159
BPHE357
BTHR384
BASP386
BARG430
BMG800
BHOH811
BHOH836
BHOH901
BHOH902
BHOH903
BHOH985
BHOH1162
BHOH1167
BLEU93
BGLU117

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 800
ChainResidue
ATHR123
AHOH901
AHOH902
AHOH903
AHOH904
AADP1000

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ADP A 1000
ChainResidue
ALEU93
AGLU117
ATHR118
AGLY119
ASER120
AGLY121
ALYS122
ATHR123
ATHR124
AARG159
APHE357
ATHR384
AASP386
AARG430
AMG800
AHOH901
AHOH902
AHOH903
AHOH933
AHOH1012
AHOH1063
AHOH1141

Functional Information from PROSITE/UniProt
site_idPS00690
Number of Residues10
DetailsDEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. ScIILDEAHE
ChainResidueDetails
BSER210-GLU219

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues330
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues360
DetailsDomain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues146
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsMotif: {"description":"DEAH box"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues24
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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