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6CGL

X-ray crystal structure of Bacillus subtilis ribonucleotide reductase NrdE alpha subunit dAMP-bound as-isolated (pH 4)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005524molecular_functionATP binding
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0016491molecular_functionoxidoreductase 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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue D5M A 801
ChainResidue
AVAL33
AHIS34
APHE37
AASN42
AARG90
APHE91

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 802
ChainResidue
ASER583
AILE584
ATHR153
ATHR581
AGLY582

site_idAC3
Number of Residues2
Detailsbinding site for residue SO4 A 803
ChainResidue
AVAL367
ALYS530

site_idAC4
Number of Residues8
Detailsbinding site for residue D5M B 801
ChainResidue
AHIS49
AGLU53
BVAL33
BHIS34
BPHE37
BASN42
BARG90
BPHE91

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 B 802
ChainResidue
BTHR153
BPRO580
BGLY582
BSER583
BILE584

site_idAC6
Number of Residues2
Detailsbinding site for residue SO4 B 803
ChainResidue
BVAL367
BLYS530

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 B 804
ChainResidue
AASN338
ALYS341
BTYR606
BGLY607

Functional Information from PROSITE/UniProt
site_idPS00089
Number of Residues23
DetailsRIBORED_LARGE Ribonucleotide reductase large subunit signature. WkkLkafvaehGMYHsyrLCiaP
ChainResidueDetails
ATRP558-PRO580

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASN380
AGLU384
BASN380
BGLU384

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Cysteine radical intermediate => ECO:0000250
ChainResidueDetails
ACYS382
BCYS382

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR153
BPRO580
ASER169
AGLY198
AASN380
APRO580
BTHR153
BSER169
BGLY198
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

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PDB entries from 2024-11-13

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