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1BIQ

RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN MUTANT E238A

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 FE2 A 376
ChainResidue
AASP84
AGLU115
AHIS118
AMTY208
AFE377
AOH378
AOH379

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 377
ChainResidue
AGLU115
AGLU204
AMTY208
AHIS241
AFE2376
AOH378

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B 376
ChainResidue
BASP84
BGLU115
BHIS118
BFE2377
BOH378

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B 377
ChainResidue
BGLU115
BGLU204
BHIS241
BFE2376
BOH378

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OH A 378
ChainResidue
AGLU115
AHIS118
AGLU204
AMTY208
AHIS241
AFE2376
AFE377
AOH379

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OH A 379
ChainResidue
AASP84
AHIS118
AMTY208
AILE234
AFE2376
AOH378

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OH B 378
ChainResidue
BGLU115
BHIS118
BGLU204
BALA238
BHIS241
BFE2376
BFE2377

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 380
ChainResidue
ATYR156
ATYR157
ACYS196
AVAL200
AHG385

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 379
ChainResidue
BTYR157
BCYS196
BVAL200
BHG381

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 380
ChainResidue
BTYR194
BLEU195
BCYS268
BCYS272

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 381
ChainResidue
BTYR156
BTYR157
BCYS196
BVAL200
BHG379

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 381
ChainResidue
ATYR194
ALEU195
ACYS268
ACYS272

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 382
ChainResidue
BILE72
BCYS214
BPHE218
BMET296

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 382
ChainResidue
ATYR194
AALA265
ACYS272

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 383
ChainResidue
AVAL210
AALA213
ACYS214
ALEU304
AHG386

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 384
ChainResidue
ALYS284
ACYS305
AGLN306
AGLU309

site_idBC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG B 383
ChainResidue
BTYR194

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG B 384
ChainResidue
BCYS305
BGLU309

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG B 385
ChainResidue
BMET198
BCYS272

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 386
ChainResidue
BVAL210
BALA213
BCYS214
BLEU304
BHG387

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 387
ChainResidue
BASN76
BVAL210
BCYS214
BHG386

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 385
ChainResidue
ATYR157
ACYS196
ALEU197
AVAL200
AHG380

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 386
ChainResidue
AASN76
AVAL210
ACYS214
ALEU290
AHG383

site_idFE1
Number of Residues7
DetailsDIIRON CLUSTER IN CHAIN A.
ChainResidue
AASP84
AGLU115
AHIS118
AGLU204
AHIS241
BFE2376
BFE2377

site_idFE2
Number of Residues7
DetailsDIIRON CLUSTER IN CHAIN B.
ChainResidue
BHIS118
BGLU204
BHIS241
AFE2376
AFE377
BASP84
BGLU115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
BTHR123

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
BSER85
BTHR116
BSER119
BALA205
BALA239
BLEU242

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
BPHE122

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
APHE122

site_idMCSA1
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
BTHR123pi-pi interaction, single electron relay
BALA238

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PDB entries from 2024-07-24

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