Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
C0005524molecular_functionATP binding
C0005971cellular_componentribonucleoside-diphosphate reductase complex
C0009263biological_processdeoxyribonucleotide biosynthetic process
C0016491molecular_functionoxidoreductase activity
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic 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
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 Residues22
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

244349

PDB entries from 2025-11-05

PDB statisticsPDBj update infoContact PDBjnumon