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2RIO

Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing

Functional Information from GO Data
ChainGOidnamespacecontents
A0004521molecular_functionRNA endonuclease activity
A0004540molecular_functionRNA nuclease activity
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006397biological_processmRNA processing
A0006468biological_processprotein phosphorylation
A0030968biological_processendoplasmic reticulum unfolded protein response
B0004521molecular_functionRNA endonuclease activity
B0004540molecular_functionRNA nuclease activity
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006397biological_processmRNA processing
B0006468biological_processprotein phosphorylation
B0030968biological_processendoplasmic reticulum unfolded protein response
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 1102
ChainResidue
AASN145
AASP171
AADP1101

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SR A 1103
ChainResidue
AASP171
AADP1101

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 2102
ChainResidue
BASN145
BASP171
BADP2101

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SR B 2103
ChainResidue
BADP2101
BASP171

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP A 1101
ChainResidue
AGLY24
ATYR25
AGLY26
ASER27
ATHR30
AVAL32
AALA43
ALYS45
ALEU88
AGLU89
ACYS91
AASN94
AGLN144
AASN145
ALEU147
AASP171
AMG1102
ASR1103

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP B 2101
ChainResidue
BGLY24
BTYR25
BGLY26
BSER27
BTHR30
BVAL32
BALA43
BLYS45
BILE72
BGLU89
BCYS91
BASN94
BGLN144
BASN145
BLEU147
BASP171
BMG2102
BSR2103

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpqNILV
ChainResidueDetails
AILE136-VAL148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP140
BASP140

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU23
BLEU23

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS45
BLYS45

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000305|PubMed:8670804
ChainResidueDetails
ASER183
ASER184
BSER183
BSER184

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP140
AGLN144

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP140
BGLN144

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS142
AASP140

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS142
BASP140

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS142
ATHR195
AASP140

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS142
BTHR195
BASP140

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS142
AASN145
AASP140

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS142
BASN145
BASP140

225158

PDB entries from 2024-09-18

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