Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000210 | molecular_function | NAD+ diphosphatase activity |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0006402 | biological_process | mRNA catabolic process |
A | 0006734 | biological_process | NADH metabolic process |
A | 0006742 | biological_process | NADP catabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019677 | biological_process | NAD catabolic process |
A | 0030145 | molecular_function | manganese ion binding |
A | 0035529 | molecular_function | NADH pyrophosphatase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0048255 | biological_process | mRNA stabilization |
A | 0110153 | molecular_function | RNA NAD-cap (NMN-forming) hydrolase activity |
A | 0110155 | biological_process | NAD-cap decapping |
B | 0000210 | molecular_function | NAD+ diphosphatase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0006402 | biological_process | mRNA catabolic process |
B | 0006734 | biological_process | NADH metabolic process |
B | 0006742 | biological_process | NADP catabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019677 | biological_process | NAD catabolic process |
B | 0030145 | molecular_function | manganese ion binding |
B | 0035529 | molecular_function | NADH pyrophosphatase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0048255 | biological_process | mRNA stabilization |
B | 0110153 | molecular_function | RNA NAD-cap (NMN-forming) hydrolase activity |
B | 0110155 | biological_process | NAD-cap decapping |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 500 |
Chain | Residue |
A | CYS98 |
A | CYS101 |
A | CYS116 |
A | CYS119 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue NAD A 501 |
Chain | Residue |
A | SER199 |
A | MET201 |
A | THR239 |
A | VAL240 |
A | ALA241 |
A | HOH602 |
A | HOH629 |
B | LYS25 |
B | GLU111 |
B | TYR124 |
A | ALA128 |
A | PHE160 |
A | GLN192 |
A | TRP194 |
A | PHE196 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 500 |
Chain | Residue |
B | CYS98 |
B | CYS101 |
B | CYS116 |
B | CYS119 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue NAD B 501 |
Chain | Residue |
A | TYR124 |
A | HOH626 |
B | ALA128 |
B | CYS130 |
B | PHE160 |
B | TRP194 |
B | PHE196 |
B | MET201 |
B | THR239 |
B | VAL240 |
B | ALA241 |
Functional Information from PROSITE/UniProt
site_id | PS00893 |
Number of Residues | 22 |
Details | NUDIX_BOX Nudix box signature. GfvevgEtleqAVaREVmEEsG |
Chain | Residue | Details |
A | GLY159-GLY180 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS25 | |
B | LYS25 | |
Chain | Residue | Details |
A | ARG69 | |
B | ARG69 | |
Chain | Residue | Details |
A | CYS98 | |
A | CYS101 | |
A | CYS116 | |
A | CYS119 | |
B | CYS98 | |
B | CYS101 | |
B | CYS116 | |
B | CYS119 | |
Chain | Residue | Details |
A | GLU111 | |
B | GLU111 | |
Chain | Residue | Details |
A | TYR124 | |
A | GLN192 | |
A | ALA241 | |
B | TYR124 | |
B | GLN192 | |
B | ALA241 | |
Chain | Residue | Details |
A | ALA158 | |
A | GLU174 | |
A | GLU178 | |
A | GLU219 | |
B | ALA158 | |
B | GLU174 | |
B | GLU178 | |
B | GLU219 | |