3CJR
Ribosomal protein L11 methyltransferase (PrmA) in complex with ribosomal protein L11 (K39A) and inhibitor Sinefungin.
Functional 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 | 0005515 | molecular_function | protein binding |
| 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 | 19 |
| Details | BINDING SITE FOR RESIDUE SFG A 255 |
| Chain | Residue |
| A | PHE99 |
| A | SER175 |
| A | ASN191 |
| A | LEU192 |
| A | HOH285 |
| A | HOH286 |
| A | HOH314 |
| A | HOH375 |
| A | HOH469 |
| A | HOH473 |
| A | HOH497 |
| A | GLY100 |
| A | THR107 |
| A | GLY128 |
| A | THR129 |
| A | LEU134 |
| A | ASP149 |
| A | ILE150 |
| A | GLY174 |
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 |
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 |
