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1PJ1

RIBONUCLEOTIDE REDUCTASE R2-D84E/W48F SOAKED WITH FERROUS IONS AT PH 5

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 406
ChainResidue
AGLU84
AGLU115
AHIS118
AGLU238

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 407
ChainResidue
ATRP111
AGLU115
AGLU204
AGLU238
AHIS241

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE B 408
ChainResidue
BGLU84
BGLU115
BHIS118
BGLU238

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 409
ChainResidue
BGLU115
BGLU204
BPHE208
BGLU238
BHIS241

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 408
ChainResidue
ATYR194
AALA265
ACYS272

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 409
ChainResidue
ATYR157
ACYS196
AHG413

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 410
ChainResidue
AVAL210
ACYS214

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 410
ChainResidue
BTYR156
BTYR157
BCYS196
BVAL200
BHG417

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 411
ChainResidue
BTYR194
BLEU195
BCYS268
BCYS272
BHOH512

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 412
ChainResidue
BVAL210
BALA213
BCYS214
BLEU304

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 411
ChainResidue
ACYS305
AGLU309

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 413
ChainResidue
BMET198
BCYS272
BLEU275
BPHE276

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 412
ChainResidue
ALYS191
ACYS268

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 414
ChainResidue
BLYS284
BCYS305
BGLU309
BHG416

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 415
ChainResidue
BILE72
BCYS214
BPHE218
BMET296
BLEU299

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 416
ChainResidue
BCYS305
BGLN306
BGLU309
BHG414

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 417
ChainResidue
BTYR157
BCYS196
BVAL200
BHG410

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 413
ChainResidue
ATYR157
ACYS196
AHG409

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 414
ChainResidue
ATYR194
ALEU195
ACYS268
ACYS272

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

225158

PDB entries from 2024-09-18

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