Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1PFR

RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN

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 A 501
ChainResidue
AASP84
AGLU115
AHIS118
AGLU238

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 502
ChainResidue
AGLU115
AGLU204
AGLU238
AHIS241

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG A 601
ChainResidue
ATYR156
ATYR157
ACYS196
AVAL200
AHG603
AHOH612

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 602
ChainResidue
ATYR194
AMET198
AALA265
ACYS272
AHOH667

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 603
ChainResidue
ATYR157
ACYS196
ALEU197
AVAL200
AHG601

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 604
ChainResidue
ACYS268
AHOH695

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 503
ChainResidue
BASP84
BGLU115
BHIS118
BGLU238
BFE504

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE B 504
ChainResidue
BGLU115
BGLU204
BGLU238
BHIS241
BFE503
BHOH663

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG B 605
ChainResidue
BTYR156
BTYR157
BCYS196
BVAL200
BHG606
BHOH617

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 606
ChainResidue
BTYR157
BCYS196
BVAL200
BHG605

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG B 607
ChainResidue
BTYR194
BCYS268
BCYS272

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG B 608
ChainResidue
BILE72
BCYS214
BMET296

site_idFE1
Number of Residues6
DetailsDIFERROUS IRON CENTER IN SUBUNIT A.
ChainResidue
AASP84
AGLU115
AHIS118
AGLU204
AGLU238
AHIS241

site_idFE2
Number of Residues6
DetailsDIFERROUS IRON CENTER IN SUBUNIT B.
ChainResidue
BGLU204
BGLU238
BHIS241
BASP84
BGLU115
BHIS118

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
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

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
ATYR122pi-pi interaction, single electron relay
AASP237

site_idMCSA2
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
BTYR122pi-pi interaction, single electron relay
BASP237

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon