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1MXR

High resolution structure of Ribonucleotide reductase R2 from E. coli in its oxidised (Met) form

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 Residues6
DetailsBINDING SITE FOR RESIDUE FE B 1001
ChainResidue
BASP84
BGLU115
BHIS118
BFE1002
BHOH2055
BHOH2388

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE B 1002
ChainResidue
BHIS241
BFE1001
BHOH2031
BHOH2388
BGLU115
BGLU204
BGLU238

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 1003
ChainResidue
AASP84
AGLU115
AHIS118
AFE1004
AHOH3051
AHOH3440

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE A 1004
ChainResidue
AGLU115
AGLU204
AGLU238
AHIS241
AFE1003
AHOH3041
AHOH3440

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 2001
ChainResidue
ATYR157
ACYS196
AVAL200
AHOH3069
AHOH3382

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 2002
ChainResidue
BTYR157
BCYS196
BVAL200
BHG2003

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG B 2003
ChainResidue
BTYR156
BTYR157
BCYS196
BVAL200
BHG2002
BHOH2091

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 2004
ChainResidue
ATYR194
AALA265
ACYS272
AHOH3059

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 2005
ChainResidue
AVAL210
ACYS214
AHOH3417
AHOH3441

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 2006
ChainResidue
BVAL210
BALA213
BCYS214
BLEU304
BHG2007

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 2007
ChainResidue
BVAL210
BCYS214
BLEU290
BHG2006
BHOH2159

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 2008
ChainResidue
BMET198
BCYS272
BPHE276
BHOH2198
BHOH2222

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 2009
ChainResidue
ACYS305
AGLU309
AHOH3278
AHOH3328

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG B 2010
ChainResidue
BTYR194
BALA265
BHOH2028

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG B 2011
ChainResidue
BLYS284
BCYS305
BGLU309

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 3001
ChainResidue
AALA217
AGLU220
AARG221
AILE297
AGLY298
ATRP334
AHOH3186
BHOH2064
BHOH2089

Functional Information from PROSITE/UniProt
site_idPS00368
Number of Residues17
DetailsRIBORED_SMALL Ribonucleotide reductase small subunit signature. SEt.IHSrSYthIirnIV
ChainResidueDetails
ASER114-VAL130

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
ATYR122

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
BTYR122

site_idMCSA1
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
ATHR123pi-pi interaction, single electron relay
AGLU238

site_idMCSA2
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
BTHR123pi-pi interaction, single electron relay
BGLU238

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PDB entries from 2024-10-16

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