1G9Q
COMPLEX STRUCTURE OF THE ADPR-ASE AND ITS SUBSTRATE ADP-RIBOSE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0006753 | biological_process | nucleoside phosphate metabolic process |
A | 0009408 | biological_process | response to heat |
A | 0016462 | molecular_function | pyrophosphatase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
A | 0019144 | molecular_function | ADP-sugar diphosphatase activity |
A | 0019693 | biological_process | ribose phosphate metabolic process |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047631 | molecular_function | ADP-ribose diphosphatase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0006753 | biological_process | nucleoside phosphate metabolic process |
B | 0009408 | biological_process | response to heat |
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 | 0019144 | molecular_function | ADP-sugar diphosphatase activity |
B | 0019693 | biological_process | ribose phosphate metabolic process |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047631 | molecular_function | ADP-ribose diphosphatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE APR B 301 |
Chain | Residue |
A | GLU17 |
A | GLU139 |
A | SER141 |
A | HOH217 |
A | HOH246 |
A | HOH252 |
B | ARG50 |
B | ARG51 |
B | GLU52 |
B | SER133 |
B | GLY135 |
A | ILE18 |
B | HOH332 |
B | HOH385 |
A | ILE19 |
A | PHE28 |
A | PHE29 |
A | ARG37 |
A | ARG56 |
A | ARG79 |
A | MET98 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE APR B 302 |
Chain | Residue |
A | ARG51 |
A | GLU52 |
A | SER133 |
A | GLY135 |
B | PHE28 |
B | PHE29 |
B | ARG56 |
B | ARG79 |
B | ALA96 |
B | GLY97 |
B | MET98 |
B | GLU112 |
B | GLU139 |
B | ASN163 |
B | HOH303 |
B | HOH327 |
B | HOH353 |
B | HOH407 |
Functional Information from PROSITE/UniProt
site_id | PS00893 |
Number of Residues | 22 |
Details | NUDIX_BOX Nudix box signature. GmieegEsvedVArREAiEEaG |
Chain | Residue | Details |
A | GLY97-GLY118 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305 |
Chain | Residue | Details |
A | GLU162 | |
B | GLU162 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: in other chain |
Chain | Residue | Details |
A | PHE28 | |
B | GLU139 | |
A | ARG56 | |
A | ARG79 | |
A | MET98 | |
A | GLU139 | |
B | PHE28 | |
B | ARG56 | |
B | ARG79 | |
B | MET98 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG51 | |
B | GLU116 | |
B | SER133 | |
B | GLU164 | |
A | ALA96 | |
A | GLU112 | |
A | GLU116 | |
A | SER133 | |
A | GLU164 | |
B | ARG51 | |
B | ALA96 | |
B | GLU112 |