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6EBZ

Crystal Structure of the Class Ie Ribonucleotide Reductase Beta Subunit from Aerococcus urinae in Activated Form with Thiocyanate Bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005829cellular_componentcytosol
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005829cellular_componentcytosol
B0005971cellular_componentribonucleoside-diphosphate reductase complex
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
C0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
C0005829cellular_componentcytosol
C0005971cellular_componentribonucleoside-diphosphate reductase complex
C0009263biological_processdeoxyribonucleotide biosynthetic process
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
D0005829cellular_componentcytosol
D0005971cellular_componentribonucleoside-diphosphate reductase complex
D0009263biological_processdeoxyribonucleotide biosynthetic process
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA A 401
ChainResidue
AGLY263
AGLU267
AHOH623
BGLY261
BHOH639

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 402
ChainResidue
BLEU264
BALA265
BHOH612
AASP260
BHIS256
BTYR259
BASP260

site_idAC3
Number of Residues1
Detailsbinding site for residue SCN B 401
ChainResidue
BPHE241

site_idAC4
Number of Residues7
Detailsbinding site for residue SCN B 402
ChainResidue
BLEU84
BASP85
BGLN88
BMET175
BPRO176
BLEU180
BLYS210

site_idAC5
Number of Residues4
Detailsbinding site for residue SCN B 403
ChainResidue
AGLU137
BTYR5
BASN28
BLYS31

site_idAC6
Number of Residues7
Detailsbinding site for residue CA B 404
ChainResidue
BSER128
BHOH551
BHOH582
BHOH585
BHOH666
CHOH545
CHOH557

site_idAC7
Number of Residues6
Detailsbinding site for residue CA B 405
ChainResidue
AGLY261
AHOH648
BGLY263
BGLU267
BHOH591
BHOH628

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 406
ChainResidue
BASP68
BASP69
CLYS232
CGLU235

site_idAC9
Number of Residues2
Detailsbinding site for residue SCN C 401
ChainResidue
CPHE241
CHOH624

site_idAD1
Number of Residues8
Detailsbinding site for residue SCN C 402
ChainResidue
CASP260
CGLY263
CALA265
CASP266
CGLU267
CCA404
DASP260
DGLY261

site_idAD2
Number of Residues6
Detailsbinding site for residue CA C 403
ChainResidue
BHOH560
BHOH592
CSER128
CHOH561
CHOH587
CHOH648

site_idAD3
Number of Residues6
Detailsbinding site for residue CA C 404
ChainResidue
CGLY263
CGLU267
CSCN402
CHOH601
DGLY261
DHOH620

site_idAD4
Number of Residues6
Detailsbinding site for residue CA D 401
ChainResidue
CGLY261
DGLY263
DASP266
DGLU267
DHOH607
DHOH621

site_idAD5
Number of Residues15
Detailsbinding site for Ligand residues DAH A 123 through GLY A 124 bound to SER A 122
ChainResidue
APHE78
ALEU81
ATHR82
AASP85
AHIS119
AALA120
AARG121
ASER122
ATHR125
AILE126
APHE127
ASER128
APHE184
AILE206
BASN30

site_idAD6
Number of Residues15
Detailsbinding site for Ligand residues DAH B 123 through GLY B 124 bound to SER B 122
ChainResidue
AASN30
BLEU81
BTHR82
BASP85
BHIS119
BALA120
BARG121
BSER122
BTHR125
BILE126
BPHE127
BSER128
BPHE184
BHOH515
BHOH558

site_idAD7
Number of Residues15
Detailsbinding site for Ligand residues DAH C 123 through GLY C 124 bound to SER C 122
ChainResidue
CLEU81
CTHR82
CASP85
CHIS119
CALA120
CARG121
CSER122
CTHR125
CILE126
CPHE127
CSER128
CPHE184
CILE206
CHOH501
DASN30

site_idAD8
Number of Residues14
Detailsbinding site for Ligand DAH C 123 bound to SER C 122
ChainResidue
CLEU81
CTHR82
CASP85
CHIS119
CALA120
CARG121
CSER122
CGLY124
CTHR125
CILE126
CPHE127
CPHE184
CILE206
CHOH501

site_idAD9
Number of Residues15
Detailsbinding site for Ligand residues DAH D 123 through GLY D 124 bound to SER D 122
ChainResidue
CASN30
DLEU81
DTHR82
DASP85
DHIS119
DALA120
DARG121
DSER122
DTHR125
DILE126
DPHE127
DSER128
DPHE184
DHOH501
DHOH505

218853

PDB entries from 2024-04-24

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