3EGV
Ribosomal protein L11 methyltransferase (PrmA) in complex with trimethylated ribosomal protein L11
Replaces: 3CJUFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006479 | biological_process | protein methylation |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008276 | molecular_function | protein methyltransferase activity |
| A | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003735 | molecular_function | structural constituent of ribosome |
| B | 0005840 | cellular_component | ribosome |
| B | 0006412 | biological_process | translation |
| B | 0015934 | cellular_component | large ribosomal subunit |
| B | 0019843 | molecular_function | rRNA binding |
| B | 0022625 | cellular_component | cytosolic large ribosomal subunit |
| B | 0070180 | molecular_function | large ribosomal subunit rRNA binding |
| B | 1990904 | cellular_component | ribonucleoprotein complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH A 301 |
| Chain | Residue |
| A | PHE99 |
| A | ASP151 |
| A | SER175 |
| A | ASN191 |
| A | LEU192 |
| A | LEU196 |
| A | HOH572 |
| A | HOH721 |
| A | HOH723 |
| A | HOH732 |
| A | HOH738 |
| A | GLY100 |
| A | HOH739 |
| A | HOH746 |
| B | 4MM1 |
| A | THR107 |
| A | GLY128 |
| A | THR129 |
| A | GLY130 |
| A | LEU134 |
| A | ASP149 |
| A | ILE150 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | PRO120 |
| A | GLU159 |
| A | ARG170 |
| A | PHE171 |
| A | HOH503 |
| A | HOH628 |
| A | HOH656 |
| A | HOH668 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | ALA115 |
| A | ARG116 |
| A | LEU118 |
| A | LYS123 |
| A | ALA145 |
| A | LEU146 |
| A | ARG170 |
| A | PHE182 |
| A | HOH612 |
| A | HOH614 |
| A | HOH728 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 304 |
| Chain | Residue |
| A | ARG116 |
| A | HIS117 |
| A | GLY183 |
| A | PRO184 |
| A | ASP186 |
| A | VAL209 |
| A | GLU240 |
| A | HOH532 |
| A | HOH607 |
| A | HOH609 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 305 |
| Chain | Residue |
| A | ARG65 |
| A | LYS68 |
| A | PRO69 |
| A | HIS82 |
| A | THR83 |
| A | HOH745 |
| A | HOH755 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 306 |
| Chain | Residue |
| A | HOH465 |
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 | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00735","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17215866","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18611379","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of ribosomal protein L11 methyltransferase from Thermus thermophilus.","authors":["Kaminishi T.","Sakai H.","Takemoto-Hori C.","Terada T.","Nakagawa N.","Maoka N.","Kuramitsu S.","Shirouzu M.","Yokoyama S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17215866","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18611379","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of ribosomal protein L11 methyltransferase from Thermus thermophilus.","authors":["Kaminishi T.","Sakai H.","Takemoto-Hori C.","Terada T.","Nakagawa N.","Maoka N.","Kuramitsu S.","Shirouzu M.","Yokoyama S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"10333296","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"18611379","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3EGV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"UniProtKB","id":"P0A7J7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |






