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6MW3

EM structure of Bacillus subtilis ribonucleotide reductase inhibited filament composed of NrdE alpha subunit and NrdF beta subunit with dATP

Functional Information from GO Data
ChainGOidnamespacecontents
C0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
C0005524molecular_functionATP binding
C0005971cellular_componentribonucleoside-diphosphate reductase complex
C0009263biological_processdeoxyribonucleotide biosynthetic process
C0016491molecular_functionoxidoreductase activity
D0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
D0005524molecular_functionATP binding
D0005971cellular_componentribonucleoside-diphosphate reductase complex
D0009263biological_processdeoxyribonucleotide biosynthetic process
D0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue DTP C 1001
ChainResidue
CASP177
CSER178
CLEU179
CARG207
CILE213
CLYS214
DLYS194
DTYR236
DALA237

site_idAC2
Number of Residues6
Detailsbinding site for residue DTP C 1002
ChainResidue
CVAL33
CHIS34
CPHE37
CASN42
CARG90
CPHE91

site_idAC3
Number of Residues9
Detailsbinding site for residue DTP D 1001
ChainResidue
CLYS194
CTYR236
CALA237
DASP177
DSER178
DLEU179
DARG207
DILE213
DLYS214

site_idAC4
Number of Residues6
Detailsbinding site for residue DTP D 1002
ChainResidue
DVAL33
DHIS34
DPHE37
DASN42
DARG90
DPHE91

Functional Information from PROSITE/UniProt
site_idPS00089
Number of Residues23
DetailsRIBORED_LARGE Ribonucleotide reductase large subunit signature. WkkLkafvaehGMYHsyrLCiaP
ChainResidueDetails
CTRP558-PRO580

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
CASN380
CGLU384
DASN380
DGLU384

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Cysteine radical intermediate => ECO:0000250
ChainResidueDetails
CCYS382
DCYS382

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
CTHR153
DPRO580
CSER169
CGLY198
CASN380
CPRO580
DTHR153
DSER169
DGLY198
DASN380

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Important for hydrogen atom transfer => ECO:0000250
ChainResidueDetails
CCYS170
CCYS409
DCYS170
DCYS409

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Allosteric effector binding => ECO:0000250
ChainResidueDetails
CASP177
CARG207
DASP177
DARG207

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Important for electron transfer => ECO:0000250
ChainResidueDetails
CTYR683
CTYR684
DTYR683
DTYR684

site_idSWS_FT_FI7
Number of Residues4
DetailsSITE: Interacts with thioredoxin/glutaredoxin => ECO:0000250
ChainResidueDetails
CCYS695
CCYS698
DCYS695
DCYS698

223532

PDB entries from 2024-08-07

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