4FZV
Crystal structure of the human MTERF4:NSUN4:SAM ternary complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000957 | biological_process | mitochondrial RNA catabolic process |
A | 0001510 | biological_process | RNA methylation |
A | 0005515 | molecular_function | protein binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005762 | cellular_component | mitochondrial large ribosomal subunit |
A | 0006364 | biological_process | rRNA processing |
A | 0006396 | biological_process | RNA processing |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008173 | molecular_function | RNA methyltransferase activity |
A | 0008649 | molecular_function | rRNA methyltransferase activity |
A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
A | 0009383 | molecular_function | rRNA (cytosine-C5-)-methyltransferase activity |
A | 0016428 | molecular_function | tRNA (cytidine-5-)-methyltransferase activity |
A | 0019843 | molecular_function | rRNA binding |
A | 0031167 | biological_process | rRNA methylation |
A | 0032259 | biological_process | methylation |
A | 0042254 | biological_process | ribosome biogenesis |
A | 0062152 | molecular_function | mRNA (cytidine-5-)-methyltransferase activity |
A | 1900864 | biological_process | mitochondrial RNA modification |
B | 0003690 | molecular_function | double-stranded DNA binding |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE SAM A 401 |
Chain | Residue |
A | LEU180 |
A | LEU205 |
A | SER206 |
A | ARG209 |
A | ASP237 |
A | GLY238 |
A | ASP255 |
A | VAL256 |
A | PRO257 |
A | HOH503 |
A | HOH584 |
A | CYS181 |
A | HOH610 |
A | HOH685 |
A | HOH700 |
A | HOH773 |
A | ALA182 |
A | ALA183 |
A | PRO185 |
A | GLY185 |
A | GLY186 |
A | LYS187 |
A | ASP204 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A 402 |
Chain | Residue |
A | LEU312 |
A | ASN317 |
A | GLU318 |
A | HOH605 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 403 |
Chain | Residue |
A | GLN290 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01023, ECO:0000269|PubMed:22949673 |
Chain | Residue | Details |
A | CYS310 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
A | CYS181 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01023, ECO:0000269|PubMed:23022348 |
Chain | Residue | Details |
A | ASP237 | |
A | ASP255 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER206 |