5YGU
Crystal structure of Escherichia coli (strain K12) mRNA Decapping Complex RppH-DapF
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 | 0008047 | molecular_function | enzyme activator activity |
| A | 0008837 | molecular_function | diaminopimelate epimerase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006402 | biological_process | mRNA catabolic process |
| B | 0008033 | biological_process | tRNA processing |
| B | 0016462 | molecular_function | pyrophosphatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| B | 0034353 | molecular_function | mRNA 5'-diphosphatase activity |
| B | 0050779 | biological_process | RNA destabilization |
| B | 0110153 | molecular_function | RNA NAD-cap (NMN-forming) hydrolase activity |
| B | 0110154 | biological_process | RNA decapping |
| B | 0110155 | biological_process | NAD-cap decapping |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue TLA A 301 |
| Chain | Residue |
| A | GLN72 |
| A | ASN157 |
| A | ASN190 |
| A | GLU208 |
| A | ARG209 |
| A | CYS217 |
| A | SER219 |
| A | HOH404 |
| A | HOH420 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 303 |
| Chain | Residue |
| A | HOH460 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 304 |
| Chain | Residue |
| A | HIS201 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 305 |
| Chain | Residue |
| A | ASN133 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 306 |
| Chain | Residue |
| A | GLU69 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 308 |
| Chain | Residue |
| A | ASN11 |
| A | ARG78 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 309 |
| Chain | Residue |
| A | ARG82 |
| A | ARG85 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue IOD A 310 |
| Chain | Residue |
| A | THR99 |
| A | ASN101 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 201 |
| Chain | Residue |
| B | ARG134 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 202 |
| Chain | Residue |
| B | GLN95 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00197 |
| Chain | Residue | Details |
| A | CYS73 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00197 |
| Chain | Residue | Details |
| A | CYS217 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00197 |
| Chain | Residue | Details |
| A | ASN190 | |
| A | GLU208 | |
| A | GLY218 | |
| A | ASN11 | |
| A | GLN44 | |
| A | ASN64 | |
| A | GLY74 | |
| A | ASN157 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000255|HAMAP-Rule:MF_00197 |
| Chain | Residue | Details |
| A | HIS159 | |
| A | GLU208 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Important for dimerization => ECO:0000269|PubMed:23426375 |
| Chain | Residue | Details |
| A | TYR268 |
