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6FZ6

Crystal Structure of a radical SAM methyltransferase from Sphaerobacter thermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0002935molecular_functiontRNA (adenine(37)-C2)-methyltransferase activity
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0006364biological_processrRNA processing
A0008033biological_processtRNA processing
A0008168molecular_functionmethyltransferase activity
A0008173molecular_functionRNA methyltransferase activity
A0019843molecular_functionrRNA binding
A0030488biological_processtRNA methylation
A0032259biological_processmethylation
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0070040molecular_functionrRNA (adenine(2503)-C2-)-methyltransferase activity
A0070475biological_processrRNA base methylation
B0000049molecular_functiontRNA binding
B0002935molecular_functiontRNA (adenine(37)-C2)-methyltransferase activity
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0006364biological_processrRNA processing
B0008033biological_processtRNA processing
B0008168molecular_functionmethyltransferase activity
B0008173molecular_functionRNA methyltransferase activity
B0019843molecular_functionrRNA binding
B0030488biological_processtRNA methylation
B0032259biological_processmethylation
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
B0070040molecular_functionrRNA (adenine(2503)-C2-)-methyltransferase activity
B0070475biological_processrRNA base methylation
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue SF4 A 401
ChainResidue
ACYS110
AVAL112
AGLY113
ACYS114
ACYS117
AGLY120
ASER194
ASAH402

site_idAC2
Number of Residues19
Detailsbinding site for residue SAH A 402
ChainResidue
ACYS117
AMET157
AGLY158
AGLY160
AGLU161
ASER192
ATHR193
ASER215
AHIS217
AGLU257
AVAL259
ALEU290
AASN291
ASMC334
AGLY335
ASF4401
AHOH595
AHOH688
APHE116

site_idAC3
Number of Residues10
Detailsbinding site for residue GOL A 403
ChainResidue
ALEU223
AVAL264
AASP266
ASER267
AASN270
AHOH505
AHOH524
AHOH592
AHOH630
BTYR23

site_idAC4
Number of Residues1
Detailsbinding site for residue BR A 404
ChainResidue
AARG24

site_idAC5
Number of Residues8
Detailsbinding site for residue SF4 B 401
ChainResidue
BCYS110
BVAL112
BGLY113
BCYS114
BCYS117
BGLY120
BSER194
BSAH402

site_idAC6
Number of Residues18
Detailsbinding site for residue SAH B 402
ChainResidue
BPHE116
BCYS117
BMET157
BGLY158
BGLY160
BGLU161
BSER192
BTHR193
BSER215
BHIS217
BGLU257
BVAL259
BLEU290
BASN291
BSMC334
BGLY335
BSF4401
BHOH677

site_idAC7
Number of Residues1
Detailsbinding site for residue BR B 403
ChainResidue
BARG24

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PDB entries from 2024-07-31

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