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3CJR

Ribosomal protein L11 methyltransferase (PrmA) in complex with ribosomal protein L11 (K39A) and inhibitor Sinefungin.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006479biological_processprotein methylation
A0008168molecular_functionmethyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0032259biological_processmethylation
A0042054molecular_functionhistone methyltransferase activity
B0003735molecular_functionstructural constituent of ribosome
B0005515molecular_functionprotein binding
B0005840cellular_componentribosome
B0006412biological_processtranslation
B0019843molecular_functionrRNA binding
B0070180molecular_functionlarge ribosomal subunit rRNA binding
B1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE SFG A 255
ChainResidue
APHE99
ASER175
AASN191
ALEU192
AHOH285
AHOH286
AHOH314
AHOH375
AHOH469
AHOH473
AHOH497
AGLY100
ATHR107
AGLY128
ATHR129
ALEU134
AASP149
AILE150
AGLY174

Functional Information from PROSITE/UniProt
site_idPS00359
Number of Residues16
DetailsRIBOSOMAL_L11 Ribosomal protein L11 signature. RmIaGSarSMGvEVvG
ChainResidueDetails
BARG125-GLY140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000269|PubMed:17215866, ECO:0000269|PubMed:18611379, ECO:0000269|Ref.6
ChainResidueDetails
ATHR107
AGLY128
AASP149
AASN191

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17215866, ECO:0000269|PubMed:18611379, ECO:0000269|Ref.6
ChainResidueDetails
ASER175

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qam
ChainResidueDetails
AASP149
AASN191
AGLY128

219140

PDB entries from 2024-05-01

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