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1RSV

azide complex of the diferrous E238A mutant R2 subunit of ribonucleotide reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0009185biological_processribonucleoside diphosphate metabolic process
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0009265biological_process2'-deoxyribonucleotide biosynthetic process
A0015949biological_processnucleobase-containing small molecule interconversion
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005971cellular_componentribonucleoside-diphosphate reductase complex
B0009185biological_processribonucleoside diphosphate metabolic process
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0009265biological_process2'-deoxyribonucleotide biosynthetic process
B0015949biological_processnucleobase-containing small molecule interconversion
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE B 1001
ChainResidue
BASP84
BGLU115
BHIS118
BHOH2180

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE B 1002
ChainResidue
BGLU115
BGLU204
BHIS241
BHOH2180

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 1003
ChainResidue
AGLU115
AHIS118
APHE208
AAZI901
AASP84

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 1004
ChainResidue
AGLU115
AGLU204
AHIS241
AAZI901

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG A 2001
ChainResidue
ATYR156
ATYR157
ACYS196
AVAL200
AHG2008
AHOH2110

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 2002
ChainResidue
BTYR157
BCYS196
BVAL200
BHG2004
BHOH2175

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG B 2003
ChainResidue
BTYR194
BLEU195
BCYS268
BCYS272
BHOH2030
BHOH2171

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HG B 2004
ChainResidue
BTYR156
BTYR157
BCYS196
BVAL200
BHG2002
BHOH2138
BHOH2175

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 2006
ChainResidue
BILE72
BCYS214
BPHE218
BMET296

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG A 2007
ChainResidue
ATYR194
AMET198
AALA265
ACYS272
AHOH2127
BHOH2172

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 2008
ChainResidue
ATYR157
ACYS196
AVAL200
AHG2001

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG A 2009
ChainResidue
AVAL210
ACYS214
ALEU304
AHOH2147
AHOH2149
AHOH2165

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 2010
ChainResidue
BVAL210
BALA213
BCYS214
BLEU304

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 2011
ChainResidue
ACYS268
AHOH2140

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 2012
ChainResidue
ALYS284
ACYS305
AGLN306
AGLU309
AHOH2151

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 2013
ChainResidue
BMET198
BCYS272
BLEU275
BPHE276

site_idBC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE AZI A 901
ChainResidue
AGLU115
AHIS118
AGLU204
APHE208
AALA238
AHIS241
AFE1003
AFE1004

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
ATHR123
BTHR123

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
ASER85
BALA205
BALA239
BLEU242
ATHR116
ASER119
AALA205
AALA239
ALEU242
BSER85
BTHR116
BSER119

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
APHE122

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
BPHE122

site_idMCSA1
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
ATHR123pi-pi interaction, single electron relay
AALA238

site_idMCSA2
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
BTHR123pi-pi interaction, single electron relay
BALA238

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PDB entries from 2024-07-24

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