3CJT
Ribosomal protein L11 methyltransferase (PrmA) in complex with dimethylated ribosomal protein L11
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006338 | biological_process | chromatin remodeling |
A | 0006479 | biological_process | protein methylation |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008276 | molecular_function | protein methyltransferase activity |
A | 0032259 | biological_process | methylation |
A | 0042054 | molecular_function | histone methyltransferase activity |
B | 0003735 | molecular_function | structural constituent of ribosome |
B | 0005515 | molecular_function | protein binding |
B | 0005840 | cellular_component | ribosome |
B | 0006412 | biological_process | translation |
B | 0019843 | molecular_function | rRNA binding |
B | 0070180 | molecular_function | large ribosomal subunit rRNA binding |
B | 1990904 | cellular_component | ribonucleoprotein complex |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006338 | biological_process | chromatin remodeling |
C | 0006479 | biological_process | protein methylation |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0008276 | molecular_function | protein methyltransferase activity |
C | 0032259 | biological_process | methylation |
C | 0042054 | molecular_function | histone methyltransferase activity |
D | 0003735 | molecular_function | structural constituent of ribosome |
D | 0005515 | molecular_function | protein binding |
D | 0005840 | cellular_component | ribosome |
D | 0006412 | biological_process | translation |
D | 0019843 | molecular_function | rRNA binding |
D | 0070180 | molecular_function | large ribosomal subunit rRNA binding |
D | 1990904 | cellular_component | ribonucleoprotein complex |
E | 0005515 | molecular_function | protein binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006338 | biological_process | chromatin remodeling |
E | 0006479 | biological_process | protein methylation |
E | 0008168 | molecular_function | methyltransferase activity |
E | 0008276 | molecular_function | protein methyltransferase activity |
E | 0032259 | biological_process | methylation |
E | 0042054 | molecular_function | histone methyltransferase activity |
F | 0003735 | molecular_function | structural constituent of ribosome |
F | 0005515 | molecular_function | protein binding |
F | 0005840 | cellular_component | ribosome |
F | 0006412 | biological_process | translation |
F | 0019843 | molecular_function | rRNA binding |
F | 0070180 | molecular_function | large ribosomal subunit rRNA binding |
F | 1990904 | cellular_component | ribonucleoprotein complex |
G | 0005515 | molecular_function | protein binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0005829 | cellular_component | cytosol |
G | 0006338 | biological_process | chromatin remodeling |
G | 0006479 | biological_process | protein methylation |
G | 0008168 | molecular_function | methyltransferase activity |
G | 0008276 | molecular_function | protein methyltransferase activity |
G | 0032259 | biological_process | methylation |
G | 0042054 | molecular_function | histone methyltransferase activity |
H | 0003735 | molecular_function | structural constituent of ribosome |
H | 0005515 | molecular_function | protein binding |
H | 0005840 | cellular_component | ribosome |
H | 0006412 | biological_process | translation |
H | 0019843 | molecular_function | rRNA binding |
H | 0070180 | molecular_function | large ribosomal subunit rRNA binding |
H | 1990904 | cellular_component | ribonucleoprotein complex |
I | 0005515 | molecular_function | protein binding |
I | 0005737 | cellular_component | cytoplasm |
I | 0005829 | cellular_component | cytosol |
I | 0006338 | biological_process | chromatin remodeling |
I | 0006479 | biological_process | protein methylation |
I | 0008168 | molecular_function | methyltransferase activity |
I | 0008276 | molecular_function | protein methyltransferase activity |
I | 0032259 | biological_process | methylation |
I | 0042054 | molecular_function | histone methyltransferase activity |
J | 0003735 | molecular_function | structural constituent of ribosome |
J | 0005515 | molecular_function | protein binding |
J | 0005840 | cellular_component | ribosome |
J | 0006412 | biological_process | translation |
J | 0019843 | molecular_function | rRNA binding |
J | 0070180 | molecular_function | large ribosomal subunit rRNA binding |
J | 1990904 | cellular_component | ribonucleoprotein complex |
K | 0005515 | molecular_function | protein binding |
K | 0005737 | cellular_component | cytoplasm |
K | 0005829 | cellular_component | cytosol |
K | 0006338 | biological_process | chromatin remodeling |
K | 0006479 | biological_process | protein methylation |
K | 0008168 | molecular_function | methyltransferase activity |
K | 0008276 | molecular_function | protein methyltransferase activity |
K | 0032259 | biological_process | methylation |
K | 0042054 | molecular_function | histone methyltransferase activity |
L | 0003735 | molecular_function | structural constituent of ribosome |
L | 0005515 | molecular_function | protein binding |
L | 0005840 | cellular_component | ribosome |
L | 0006412 | biological_process | translation |
L | 0019843 | molecular_function | rRNA binding |
L | 0070180 | molecular_function | large ribosomal subunit rRNA binding |
L | 1990904 | cellular_component | ribonucleoprotein complex |
M | 0005515 | molecular_function | protein binding |
M | 0005737 | cellular_component | cytoplasm |
M | 0005829 | cellular_component | cytosol |
M | 0006338 | biological_process | chromatin remodeling |
M | 0006479 | biological_process | protein methylation |
M | 0008168 | molecular_function | methyltransferase activity |
M | 0008276 | molecular_function | protein methyltransferase activity |
M | 0032259 | biological_process | methylation |
M | 0042054 | molecular_function | histone methyltransferase activity |
N | 0003735 | molecular_function | structural constituent of ribosome |
N | 0005515 | molecular_function | protein binding |
N | 0005840 | cellular_component | ribosome |
N | 0006412 | biological_process | translation |
N | 0019843 | molecular_function | rRNA binding |
N | 0070180 | molecular_function | large ribosomal subunit rRNA binding |
N | 1990904 | cellular_component | ribonucleoprotein complex |
O | 0005515 | molecular_function | protein binding |
O | 0005737 | cellular_component | cytoplasm |
O | 0005829 | cellular_component | cytosol |
O | 0006338 | biological_process | chromatin remodeling |
O | 0006479 | biological_process | protein methylation |
O | 0008168 | molecular_function | methyltransferase activity |
O | 0008276 | molecular_function | protein methyltransferase activity |
O | 0032259 | biological_process | methylation |
O | 0042054 | molecular_function | histone methyltransferase activity |
P | 0003735 | molecular_function | structural constituent of ribosome |
P | 0005515 | molecular_function | protein binding |
P | 0005840 | cellular_component | ribosome |
P | 0006412 | biological_process | translation |
P | 0019843 | molecular_function | rRNA binding |
P | 0070180 | molecular_function | large ribosomal subunit rRNA binding |
P | 1990904 | cellular_component | ribonucleoprotein complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO3 B 148 |
Chain | Residue |
A | TYR193 |
B | LYS2 |
B | HOH193 |
G | ARG223 |
G | LEU226 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NO3 A 255 |
Chain | Residue |
A | TRP247 |
A | HOH462 |
B | HOH184 |
A | PHE99 |
A | ALA104 |
A | GLU105 |
A | THR106 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO3 F 148 |
Chain | Residue |
C | ARG223 |
C | LEU226 |
E | TYR193 |
F | LYS2 |
F | HOH756 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO3 E 255 |
Chain | Residue |
E | PHE99 |
E | ALA104 |
E | GLU105 |
E | THR106 |
E | TRP247 |
E | HOH379 |
E | HOH380 |
F | ALA61 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 I 255 |
Chain | Residue |
I | TYR193 |
J | LYS2 |
O | ARG223 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO3 I 256 |
Chain | Residue |
I | PHE99 |
I | ALA104 |
I | GLU105 |
I | THR106 |
I | TRP247 |
I | HOH353 |
J | ALA61 |
J | HOH164 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 N 148 |
Chain | Residue |
K | ARG223 |
K | LEU226 |
N | LYS2 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NO3 M 255 |
Chain | Residue |
M | PHE99 |
M | ALA104 |
M | GLU105 |
M | THR106 |
M | TRP247 |
M | HOH323 |
M | HOH418 |
N | ALA61 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 256 |
Chain | Residue |
A | ARG170 |
E | ARG170 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 257 |
Chain | Residue |
A | ARG170 |
E | ARG170 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL I 257 |
Chain | Residue |
I | ARG170 |
M | ARG170 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL I 258 |
Chain | Residue |
I | ARG170 |
M | ARG170 |
site_id | BC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE SAM C 302 |
Chain | Residue |
C | HIS103 |
C | THR107 |
C | GLY128 |
C | THR129 |
C | LEU134 |
C | ASP149 |
C | ILE150 |
C | ASP151 |
C | GLY174 |
C | SER175 |
C | ASN191 |
C | LEU192 |
C | LEU196 |
C | HOH311 |
C | HOH314 |
C | HOH330 |
C | HOH404 |
C | HOH449 |
site_id | BC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE SAM G 302 |
Chain | Residue |
A | HOH391 |
G | HIS103 |
G | GLY128 |
G | THR129 |
G | GLY130 |
G | SER131 |
G | LEU134 |
G | ASP149 |
G | ILE150 |
G | ASP151 |
G | GLY174 |
G | SER175 |
G | ASN191 |
G | LEU196 |
G | HOH316 |
G | HOH369 |
G | HOH378 |
G | HOH471 |
site_id | BC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE SAM K 302 |
Chain | Residue |
K | GLY174 |
K | SER175 |
K | ASN191 |
K | LEU192 |
K | LEU196 |
K | HOH317 |
K | HOH325 |
K | HOH326 |
K | HOH354 |
K | HOH386 |
K | HOH413 |
K | HOH414 |
M | HOH385 |
M | HOH392 |
K | HIS103 |
K | GLY128 |
K | THR129 |
K | SER131 |
K | LEU134 |
K | ASP149 |
K | ILE150 |
K | ASP151 |
site_id | BC7 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SAM O 302 |
Chain | Residue |
I | HOH445 |
O | HIS103 |
O | GLY128 |
O | THR129 |
O | SER131 |
O | LEU134 |
O | ASP149 |
O | ILE150 |
O | ASP151 |
O | GLY174 |
O | SER175 |
O | ASN191 |
O | LEU192 |
O | LEU196 |
O | HOH309 |
O | HOH313 |
O | HOH322 |
O | HOH342 |
O | HOH438 |
O | HOH440 |
site_id | BC8 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SAH A 258 |
Chain | Residue |
A | PHE99 |
A | GLY100 |
A | THR107 |
A | GLY128 |
A | THR129 |
A | GLY130 |
A | LEU134 |
A | ASP149 |
A | ILE150 |
A | ASP151 |
A | GLY174 |
A | SER175 |
A | ASN191 |
A | LEU192 |
A | LEU196 |
A | HOH315 |
A | HOH377 |
A | HOH426 |
A | HOH429 |
A | HOH481 |
site_id | BC9 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE SAH E 256 |
Chain | Residue |
E | PHE99 |
E | GLY100 |
E | THR107 |
E | LEU127 |
E | GLY128 |
E | THR129 |
E | GLY130 |
E | LEU134 |
E | ASP149 |
E | ILE150 |
E | ASP151 |
E | SER175 |
E | ASN191 |
E | LEU192 |
E | LEU196 |
E | HOH378 |
E | HOH383 |
E | HOH384 |
E | HOH411 |
E | HOH412 |
E | HOH500 |
F | HOH1158 |
site_id | CC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE SAH I 259 |
Chain | Residue |
I | PHE99 |
I | GLY100 |
I | THR107 |
I | GLY128 |
I | THR129 |
I | GLY130 |
I | LEU134 |
I | ASP149 |
I | ILE150 |
I | ASP151 |
I | GLY174 |
I | SER175 |
I | ASN191 |
I | LEU192 |
I | LEU196 |
I | HOH265 |
I | HOH267 |
I | HOH278 |
I | HOH284 |
I | HOH309 |
I | HOH347 |
site_id | CC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE SAH M 256 |
Chain | Residue |
M | PHE99 |
M | GLY100 |
M | THR107 |
M | GLY128 |
M | THR129 |
M | GLY130 |
M | LEU134 |
M | ASP149 |
M | ILE150 |
M | ASP151 |
M | GLY174 |
M | SER175 |
M | ASN191 |
M | LEU192 |
M | LEU196 |
M | HOH270 |
M | HOH279 |
M | HOH302 |
M | HOH320 |
M | HOH382 |
M | HOH430 |
N | HOH162 |
site_id | CC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 2MM B 149 |
Chain | Residue |
A | THR106 |
A | ASN191 |
A | LEU192 |
A | TYR193 |
A | GLY218 |
A | LEU220 |
A | TRP247 |
B | LYS2 |
B | LYS3 |
B | HOH184 |
site_id | CC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 2MM F 149 |
Chain | Residue |
E | THR106 |
E | ASN191 |
E | LEU192 |
E | GLY218 |
E | LEU220 |
E | TRP247 |
E | HOH380 |
E | HOH415 |
F | LYS2 |
F | LYS3 |
site_id | CC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 2MM J 148 |
Chain | Residue |
I | THR106 |
I | ASN191 |
I | LEU192 |
I | TYR193 |
I | GLY218 |
I | LEU220 |
I | TRP247 |
J | LYS2 |
J | LYS3 |
J | HOH164 |
site_id | CC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 2MM M 257 |
Chain | Residue |
M | THR106 |
M | ASN191 |
M | LEU192 |
M | TYR193 |
M | GLY218 |
M | LEU220 |
M | TRP247 |
N | LYS2 |
N | LYS3 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 150 |
Chain | Residue |
B | PRO13 |
B | ASP50 |
B | HOH189 |
site_id | CC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 259 |
Chain | Residue |
A | PRO210 |
A | GLY211 |
Functional Information from PROSITE/UniProt
site_id | PS00359 |
Number of Residues | 16 |
Details | RIBOSOMAL_L11 Ribosomal protein L11 signature. RmIaGSarSMGvEVvG |
Chain | Residue | Details |
B | ARG125-GLY140 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000269|PubMed:17215866, ECO:0000269|PubMed:18611379, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | THR107 | |
E | GLY128 | |
E | ASP149 | |
E | ASN191 | |
G | THR107 | |
G | GLY128 | |
G | ASP149 | |
G | ASN191 | |
I | THR107 | |
I | GLY128 | |
I | ASP149 | |
A | GLY128 | |
I | ASN191 | |
K | THR107 | |
K | GLY128 | |
K | ASP149 | |
K | ASN191 | |
M | THR107 | |
M | GLY128 | |
M | ASP149 | |
M | ASN191 | |
O | THR107 | |
A | ASP149 | |
O | GLY128 | |
O | ASP149 | |
O | ASN191 | |
A | ASN191 | |
C | THR107 | |
C | GLY128 | |
C | ASP149 | |
C | ASN191 | |
E | THR107 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17215866, ECO:0000269|PubMed:18611379, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | SER175 | |
C | SER175 | |
E | SER175 | |
G | SER175 | |
I | SER175 | |
K | SER175 | |
M | SER175 | |
O | SER175 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qam |
Chain | Residue | Details |
A | ASP149 | |
A | ASN191 | |
A | GLY128 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qam |
Chain | Residue | Details |
C | ASP149 | |
C | ASN191 | |
C | GLY128 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qam |
Chain | Residue | Details |
E | ASP149 | |
E | ASN191 | |
E | GLY128 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qam |
Chain | Residue | Details |
G | ASP149 | |
G | ASN191 | |
G | GLY128 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qam |
Chain | Residue | Details |
I | ASP149 | |
I | ASN191 | |
I | GLY128 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qam |
Chain | Residue | Details |
K | ASP149 | |
K | ASN191 | |
K | GLY128 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qam |
Chain | Residue | Details |
M | ASP149 | |
M | ASN191 | |
M | GLY128 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qam |
Chain | Residue | Details |
O | ASP149 | |
O | ASN191 | |
O | GLY128 |