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6QE0

Structure of E.coli RlmJ in complex with a bisubstrate analogue (BA2)

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
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue HZ2 A 301
ChainResidue
AHIS9
ASER100
AASP164
APRO166
ATYR167
AMET235
AHOH422
AHOH469
AHOH480
AHOH491
AHOH511
AALA10
AHOH554
AHOH560
AASP15
ALYS18
AHIS19
AASP40
AHIS42
AALA43
AGLY99

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:23945937
ChainResidueDetails
AASP164

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:23945937
ChainResidueDetails
AHIS19
AHIS42
ASER100
AGLU118
AASP143
AASP164

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Interaction with substrate rRNA => ECO:0000305
ChainResidueDetails
ATYR4

222624

PDB entries from 2024-07-17

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