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9BX8

Class 12 model for preturnover 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 Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Cysteine radical intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Important for hydrogen atom transfer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Allosteric effector binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Important for electron transfer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10014","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10014","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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