5HR6
X-ray crystal structure of C118A RlmN with cross-linked tRNA purified from Escherichia coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000049 | molecular_function | tRNA binding |
A | 0002935 | molecular_function | tRNA (adenine(37)-C2)-methyltransferase activity |
A | 0003824 | molecular_function | catalytic activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006364 | biological_process | rRNA processing |
A | 0008033 | biological_process | tRNA processing |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008173 | molecular_function | RNA methyltransferase activity |
A | 0019843 | molecular_function | rRNA binding |
A | 0030488 | biological_process | tRNA methylation |
A | 0032259 | biological_process | methylation |
A | 0046677 | biological_process | response to antibiotic |
A | 0046872 | molecular_function | metal ion binding |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
A | 0070040 | molecular_function | rRNA (adenine(2503)-C2-)-methyltransferase activity |
A | 0070475 | biological_process | rRNA base methylation |
B | 0000049 | molecular_function | tRNA binding |
B | 0002935 | molecular_function | tRNA (adenine(37)-C2)-methyltransferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006364 | biological_process | rRNA processing |
B | 0008033 | biological_process | tRNA processing |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008173 | molecular_function | RNA methyltransferase activity |
B | 0019843 | molecular_function | rRNA binding |
B | 0030488 | biological_process | tRNA methylation |
B | 0032259 | biological_process | methylation |
B | 0046677 | biological_process | response to antibiotic |
B | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0070040 | molecular_function | rRNA (adenine(2503)-C2-)-methyltransferase activity |
B | 0070475 | biological_process | rRNA base methylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue MET A 501 |
Chain | Residue |
A | MET175 |
A | 5AD503 |
A | GLY177 |
A | GLY179 |
A | GLU180 |
A | SER211 |
A | THR212 |
A | SER213 |
A | SER233 |
A | SF4502 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue SF4 A 502 |
Chain | Residue |
A | CYS125 |
A | CYS129 |
A | CYS132 |
A | SER213 |
A | MET501 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue 5AD A 503 |
Chain | Residue |
A | PHE131 |
A | CYS132 |
A | SER233 |
A | HIS235 |
A | GLU278 |
A | VAL280 |
A | ILE309 |
A | TRP311 |
A | ASN312 |
A | SMC355 |
A | GLY356 |
A | MET501 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue MG A 504 |
Chain | Residue |
A | LEU196 |
A | LEU203 |
C | A26 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue MG C 101 |
Chain | Residue |
A | HOH610 |
C | C38 |
C | G39 |
C | HOH202 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue MG C 102 |
Chain | Residue |
C | U7 |
C | C8 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue MG C 103 |
Chain | Residue |
C | U7 |
C | A13 |
C | G14 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue MET B 501 |
Chain | Residue |
B | GLY177 |
B | GLY179 |
B | GLU180 |
B | SER211 |
B | THR212 |
B | SER213 |
B | SER233 |
B | SF4502 |
B | 5AD503 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue SF4 B 502 |
Chain | Residue |
B | CYS125 |
B | LEU127 |
B | CYS129 |
B | CYS132 |
B | ALA135 |
B | SER213 |
B | MET501 |
site_id | AD1 |
Number of Residues | 13 |
Details | binding site for residue 5AD B 503 |
Chain | Residue |
B | PHE131 |
B | CYS132 |
B | SER233 |
B | HIS235 |
B | GLU278 |
B | VAL280 |
B | ILE309 |
B | TRP311 |
B | ASN312 |
B | SMC355 |
B | GLY356 |
B | MET501 |
B | HOH603 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG B 504 |
Chain | Residue |
B | LEU196 |
B | ASP198 |
B | LEU203 |
B | HOH607 |
D | A26 |
D | HOH201 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue MG D 101 |
Chain | Residue |
B | HOH614 |
D | C38 |
D | G39 |
D | HOH203 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255 |
Chain | Residue | Details |
A | GLU105 | |
B | GLU105 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: S-methylcysteine intermediate => ECO:0000269|PubMed:21415317, ECO:0000269|PubMed:21527678 |
Chain | Residue | Details |
A | SMC355 | |
B | SMC355 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: |
Chain | Residue | Details |
A | CYS125 | |
B | CYS132 | |
B | GLY179 | |
B | SER211 | |
B | SER233 | |
B | ASN312 | |
A | CYS129 | |
A | CYS132 | |
A | GLY179 | |
A | SER211 | |
A | SER233 | |
A | ASN312 | |
B | CYS125 | |
B | CYS129 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 938 |
Chain | Residue | Details |
A | GLU105 | proton shuttle (general acid/base) |
A | ALA118 | covalent catalysis |
A | CYS125 | activator, metal ligand |
A | CYS129 | metal ligand |
A | CYS132 | metal ligand |
A | SMC355 | covalent catalysis |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 938 |
Chain | Residue | Details |
B | GLU105 | proton shuttle (general acid/base) |
B | ALA118 | covalent catalysis |
B | CYS125 | activator, metal ligand |
B | CYS129 | metal ligand |
B | CYS132 | metal ligand |
B | SMC355 | covalent catalysis |