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5HR6

X-ray crystal structure of C118A RlmN with cross-linked tRNA purified from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0002935molecular_functiontRNA (adenine(37)-C2)-methyltransferase activity
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006364biological_processrRNA processing
A0008033biological_processtRNA processing
A0008168molecular_functionmethyltransferase activity
A0008173molecular_functionRNA methyltransferase activity
A0019843molecular_functionrRNA binding
A0030488biological_processtRNA methylation
A0032259biological_processmethylation
A0046677biological_processresponse to antibiotic
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
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006364biological_processrRNA processing
B0008033biological_processtRNA processing
B0008168molecular_functionmethyltransferase activity
B0008173molecular_functionRNA methyltransferase activity
B0019843molecular_functionrRNA binding
B0030488biological_processtRNA methylation
B0032259biological_processmethylation
B0046677biological_processresponse to antibiotic
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 Residues10
Detailsbinding site for residue MET A 501
ChainResidue
AMET175
A5AD503
AGLY177
AGLY179
AGLU180
ASER211
ATHR212
ASER213
ASER233
ASF4502

site_idAC2
Number of Residues5
Detailsbinding site for residue SF4 A 502
ChainResidue
ACYS125
ACYS129
ACYS132
ASER213
AMET501

site_idAC3
Number of Residues12
Detailsbinding site for residue 5AD A 503
ChainResidue
APHE131
ACYS132
ASER233
AHIS235
AGLU278
AVAL280
AILE309
ATRP311
AASN312
ASMC355
AGLY356
AMET501

site_idAC4
Number of Residues3
Detailsbinding site for residue MG A 504
ChainResidue
ALEU196
ALEU203
CA26

site_idAC5
Number of Residues4
Detailsbinding site for residue MG C 101
ChainResidue
AHOH610
CC38
CG39
CHOH202

site_idAC6
Number of Residues2
Detailsbinding site for residue MG C 102
ChainResidue
CU7
CC8

site_idAC7
Number of Residues3
Detailsbinding site for residue MG C 103
ChainResidue
CU7
CA13
CG14

site_idAC8
Number of Residues9
Detailsbinding site for residue MET B 501
ChainResidue
BGLY177
BGLY179
BGLU180
BSER211
BTHR212
BSER213
BSER233
BSF4502
B5AD503

site_idAC9
Number of Residues7
Detailsbinding site for residue SF4 B 502
ChainResidue
BCYS125
BLEU127
BCYS129
BCYS132
BALA135
BSER213
BMET501

site_idAD1
Number of Residues13
Detailsbinding site for residue 5AD B 503
ChainResidue
BPHE131
BCYS132
BSER233
BHIS235
BGLU278
BVAL280
BILE309
BTRP311
BASN312
BSMC355
BGLY356
BMET501
BHOH603

site_idAD2
Number of Residues6
Detailsbinding site for residue MG B 504
ChainResidue
BLEU196
BASP198
BLEU203
BHOH607
DA26
DHOH201

site_idAD3
Number of Residues4
Detailsbinding site for residue MG D 101
ChainResidue
BHOH614
DC38
DG39
DHOH203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255
ChainResidueDetails
AGLU105
BGLU105

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: S-methylcysteine intermediate => ECO:0000269|PubMed:21415317, ECO:0000269|PubMed:21527678
ChainResidueDetails
ASMC355
BSMC355

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING:
ChainResidueDetails
ACYS125
BCYS132
BGLY179
BSER211
BSER233
BASN312
ACYS129
ACYS132
AGLY179
ASER211
ASER233
AASN312
BCYS125
BCYS129

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 938
ChainResidueDetails
AGLU105proton shuttle (general acid/base)
AALA118covalent catalysis
ACYS125activator, metal ligand
ACYS129metal ligand
ACYS132metal ligand
ASMC355covalent catalysis

site_idMCSA2
Number of Residues6
DetailsM-CSA 938
ChainResidueDetails
BGLU105proton shuttle (general acid/base)
BALA118covalent catalysis
BCYS125activator, metal ligand
BCYS129metal ligand
BCYS132metal ligand
BSMC355covalent catalysis

223532

PDB entries from 2024-08-07

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