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1JPR

Mn substituted Ribonucleotide reductase R2 from E. coli oxidized by nitric oxide

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 Residues7
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
BASP84
BGLU115
BHIS118
BGLU238
BMN402
BHOH984
BHOH1077

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 402
ChainResidue
BGLU238
BHIS241
BMN401
BHOH984
BGLU115
BGLU204

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 403
ChainResidue
AASP84
AGLU115
AHIS118
AGLU238
AMN404
AHOH1031

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 404
ChainResidue
AGLU115
AGLU204
AGLU238
AHIS241
AMN403
AHOH964

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 901
ChainResidue
ATYR157
ACYS196
AVAL200
AHOH916
AHOH950

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 902
ChainResidue
BTYR157
BCYS196
BVAL200
BHG904

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 903
ChainResidue
BTYR194
BLEU195
BCYS268
BCYS272
BHOH920

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG B 904
ChainResidue
BTYR156
BTYR157
BCYS196
BVAL200
BHG902
BHOH936

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 906
ChainResidue
BILE72
BCYS214
BPHE218
BMET296
BHOH1202

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 907
ChainResidue
ATYR194
AALA265
ACYS272
AHOH958

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 909
ChainResidue
AVAL210
ACYS214
ALEU304

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 910
ChainResidue
BMET198
BCYS272
BLEU275
BPHE276
BHOH1254

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 911
ChainResidue
BVAL210
BALA213
BCYS214
BLEU304
BHG912

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HG B 912
ChainResidue
BASN76
BVAL210
BCYS214
BTRP286
BLEU304
BHG911
BHOH1202

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 915
ChainResidue
ACYS305
AGLN306
AGLU309
AHOH949
AHOH1289

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 916
ChainResidue
BLYS284
BCYS305
BGLU309
BHOH953

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 917
ChainResidue
BTYR194
BALA265
BHOH920
BHOH1071

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 918
ChainResidue
BLYS191
BILE264
BGLU267
BCYS268

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

222036

PDB entries from 2024-07-03

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