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6PQB

Crystal structure of aminoglycoside-resistance methyltransferase RmtC bound to S-adenosylhomocysteine (SAH)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008649molecular_functionrRNA methyltransferase activity
A0046677biological_processresponse to antibiotic
B0008649molecular_functionrRNA methyltransferase activity
B0046677biological_processresponse to antibiotic
C0008649molecular_functionrRNA methyltransferase activity
C0046677biological_processresponse to antibiotic
D0008649molecular_functionrRNA methyltransferase activity
D0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue SAH A 301
ChainResidue
ATYR60
AASP188
AILE189
APHE203
ALEU205
AGLN212
ASER107
ATHR108
AARG111
AGLY136
ACYS137
AALA138
AASP160
ALEU161

site_idAC2
Number of Residues13
Detailsbinding site for residue SAH B 301
ChainResidue
BTYR60
BSER107
BTHR108
BARG111
BGLY136
BCYS137
BALA138
BASP160
BLEU161
BASP188
BILE189
BPHE203
BGLN212

site_idAC3
Number of Residues12
Detailsbinding site for residue SAH C 301
ChainResidue
CTYR60
CSER107
CTHR108
CARG111
CGLY136
CCYS137
CALA138
CASP160
CLEU161
CASP188
CPHE203
CGLN212

site_idAC4
Number of Residues14
Detailsbinding site for residue SAH D 301
ChainResidue
DTYR60
DSER107
DTHR108
DARG111
DGLY136
DCYS137
DASP160
DGLY187
DASP188
DILE189
DPHE203
DLEU205
DLEU208
DGLN212

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

255239

PDB entries from 2026-06-17

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