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3EGV

Ribosomal protein L11 methyltransferase (PrmA) in complex with trimethylated ribosomal protein L11

Replaces:  3CJU
Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0006479biological_processprotein methylation
A0008168molecular_functionmethyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0032259biological_processmethylation
A0042054molecular_functionhistone methyltransferase activity
B0003735molecular_functionstructural constituent of ribosome
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 Residues22
DetailsBINDING SITE FOR RESIDUE SAH A 301
ChainResidue
APHE99
AASP151
ASER175
AASN191
ALEU192
ALEU196
AHOH572
AHOH721
AHOH723
AHOH732
AHOH738
AGLY100
AHOH739
AHOH746
B4MM1
ATHR107
AGLY128
ATHR129
AGLY130
ALEU134
AASP149
AILE150

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
APRO120
AGLU159
AARG170
APHE171
AHOH503
AHOH628
AHOH656
AHOH668

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AALA115
AARG116
ALEU118
ALYS123
AALA145
ALEU146
AARG170
APHE182
AHOH612
AHOH614
AHOH728

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
AARG116
AHIS117
AGLY183
APRO184
AASP186
AVAL209
AGLU240
AHOH532
AHOH607
AHOH609

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
AARG65
ALYS68
APRO69
AHIS82
ATHR83
AHOH745
AHOH755

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 306
ChainResidue
AHOH465

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 Residues1
DetailsMOD_RES: N,N,N-trimethylmethionine => ECO:0000269|PubMed:18611379, ECO:0007744|PDB:3EGV
ChainResidueDetails
B4MM1
AGLY128
AASP149
AASN191

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10333296
ChainResidueDetails
BLYS3

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:18611379, ECO:0007744|PDB:3EGV
ChainResidueDetails
BLYS39

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P0A7J7
ChainResidueDetails
BLYS70

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

222415

PDB entries from 2024-07-10

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