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9BZ3

Class 17 model for turnover condition of Bacillus subtilis ribonucleotide reductase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005524molecular_functionATP binding
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005524molecular_functionATP binding
B0005971cellular_componentribonucleoside-diphosphate reductase complex
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
C0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
C0009263biological_processdeoxyribonucleotide biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
D0009263biological_processdeoxyribonucleotide biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00089
Number of Residues23
DetailsRIBORED_LARGE Ribonucleotide reductase large subunit signature. WkkLkafvaehGMYHsyrLCiaP
ChainResidueDetails
ATRP558-PRO580

site_idPS00368
Number of Residues18
DetailsRIBORED_SMALL Ribonucleotide reductase small subunit signature. MEnaVHAkSYsnIfmtLA
ChainResidueDetails
CMET96-ALA113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10014
ChainResidueDetails
CTYR105
DTYR105
BASN380
BGLU384

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10014
ChainResidueDetails
CASP66
CHIS101
DASP66
DHIS101

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
CGLU97
BPRO580
CGLU164
CGLU198
CHIS201
DGLU97
DGLU164
DGLU198
DHIS201
BASN380

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Important for hydrogen atom transfer => ECO:0000250
ChainResidueDetails
ACYS170
ACYS409
BCYS170
BCYS409

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Allosteric effector binding => ECO:0000250
ChainResidueDetails
AASP177
AARG207
BASP177
BARG207

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Important for electron transfer => ECO:0000250
ChainResidueDetails
ATYR683
ATYR684
BTYR683
BTYR684

site_idSWS_FT_FI7
Number of Residues4
DetailsSITE: Interacts with thioredoxin/glutaredoxin => ECO:0000250
ChainResidueDetails
ACYS695
ACYS698
BCYS695
BCYS698

236620

PDB entries from 2025-05-28

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