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1SQF

The crystal structure of E. coli Fmu binary complex with S-Adenosylmethionine at 2.1 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0001510biological_processRNA methylation
A0003723molecular_functionRNA binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006355biological_processregulation of DNA-templated transcription
A0006364biological_processrRNA processing
A0008168molecular_functionmethyltransferase activity
A0008173molecular_functionRNA methyltransferase activity
A0008649molecular_functionrRNA methyltransferase activity
A0009383molecular_functionrRNA (cytosine-C5-)-methyltransferase activity
A0016434molecular_functionrRNA (cytosine) methyltransferase activity
A0031167biological_processrRNA methylation
A0032259biological_processmethylation
A0070475biological_processrRNA base methylation
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SAM A 430
ChainResidue
ACYS254
AARG282
AGLY302
AASP303
AGLY304
AASP322
APRO324
AHOH443
AHOH468
AHOH532
AALA255
AALA256
APRO257
AGLY258
AGLY259
ALYS260
AASP277
AILE278

Functional Information from PROSITE/UniProt
site_idPS01153
Number of Residues12
DetailsNOL1_NOP2_SUN NOL1/NOP2/sun family signature. FDRILlDAPCSA
ChainResidueDetails
APHE316-ALA327

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
ACYS375

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ACYS254

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:14656444
ChainResidueDetails
AASP277
AASP303
AASP322

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PDB entries from 2024-07-24

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