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6QE5

Structure of E.coli RlmJ in complex with the natural cofactor product S-adenosyl-homocysteine (SAH)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006364biological_processrRNA processing
A0008168molecular_functionmethyltransferase activity
A0008649molecular_functionrRNA methyltransferase activity
A0008988molecular_functionrRNA (adenine-N6-)-methyltransferase activity
A0015976biological_processcarbon utilization
A0032259biological_processmethylation
A0036307molecular_function23S rRNA (adenine(2030)-N(6))-methyltransferase activity
A0070475biological_processrRNA base methylation
B0003676molecular_functionnucleic acid binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006364biological_processrRNA processing
B0008168molecular_functionmethyltransferase activity
B0008649molecular_functionrRNA methyltransferase activity
B0008988molecular_functionrRNA (adenine-N6-)-methyltransferase activity
B0015976biological_processcarbon utilization
B0032259biological_processmethylation
B0036307molecular_function23S rRNA (adenine(2030)-N(6))-methyltransferase activity
B0070475biological_processrRNA base methylation
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue SAH A 301
ChainResidue
ATYR4
ASER100
AGLU118
ALEU119
AHIS120
AALA142
AASP143
AGLY144
AASP164
APRO166
AHOH426
AHIS6
AHOH428
AHOH432
AHOH473
AHOH475
ALYS18
AHIS19
ATHR41
AHIS42
AALA43
AGLY44
AGLY99

site_idAC2
Number of Residues22
Detailsbinding site for residue SAH B 301
ChainResidue
BTYR4
BHIS6
BLYS18
BHIS19
BTHR41
BHIS42
BALA43
BGLY44
BGLY99
BSER100
BGLU118
BLEU119
BHIS120
BALA142
BASP143
BGLY144
BASP164
BHOH415
BHOH419
BHOH421
BHOH453
BHOH483

Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. ILIDPPY
ChainResidueDetails
AILE161-TYR167
AILE241-TRP247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:23945937
ChainResidueDetails
AASP164
BASP164

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:23945937
ChainResidueDetails
AHIS19
BGLU118
BASP143
BASP164
AHIS42
ASER100
AGLU118
AASP143
AASP164
BHIS19
BHIS42
BSER100

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Interaction with substrate rRNA => ECO:0000305
ChainResidueDetails
ATYR4
BTYR4

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PDB entries from 2024-07-17

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