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 | 42 |
| Details | Motif: {"description":"Nudix box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"description":"in other chain"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 138 |
| Details | Domain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
