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1RIB

STRUCTURE AND FUNCTION OF THE ESCHERICHIA COLI RIBONUCLEOTIDE REDUCTASE PROTEIN R2

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 Residues8
DetailsBINDING SITE FOR RESIDUE FEO A 401
ChainResidue
AASP84
AGLU115
AHIS118
AGLU204
AGLU238
AHIS241
AHOH522
AHOH749

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FEO B 402
ChainResidue
BGLU115
BHIS118
BGLU204
BGLU238
BHIS241
BHOH640
BHOH712
BASP84

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 2024-07-31

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