6DBZ
Crystal structure of Nudix 1 from Arabidopsis thaliana complexed with isopentenyl diphosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000210 | molecular_function | NAD+ diphosphatase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006974 | biological_process | DNA damage response |
A | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019177 | molecular_function | dihydroneopterin triphosphate pyrophosphohydrolase activity |
A | 0035529 | molecular_function | NADH pyrophosphatase activity |
A | 0035539 | molecular_function | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000210 | molecular_function | NAD+ diphosphatase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006974 | biological_process | DNA damage response |
B | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019177 | molecular_function | dihydroneopterin triphosphate pyrophosphohydrolase activity |
B | 0035529 | molecular_function | NADH pyrophosphatase activity |
B | 0035539 | molecular_function | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue IPR A 201 |
Chain | Residue |
A | ARG27 |
A | MG203 |
A | MG204 |
A | HOH301 |
A | HOH377 |
A | GLY40 |
A | GLY41 |
A | HIS42 |
A | GLU56 |
A | GLU60 |
A | TYR87 |
A | PHE127 |
A | MG202 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue MG A 202 |
Chain | Residue |
A | GLY40 |
A | GLU56 |
A | GLU60 |
A | IPR201 |
A | MG203 |
A | MG204 |
A | HOH301 |
A | HOH324 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 203 |
Chain | Residue |
A | GLY40 |
A | GLU60 |
A | IPR201 |
A | MG202 |
A | HOH377 |
A | HOH379 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue MG A 204 |
Chain | Residue |
A | GLU56 |
A | IPR201 |
A | MG202 |
A | HOH365 |
A | HOH380 |
A | HOH392 |
A | HOH398 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG A 205 |
Chain | Residue |
A | HOH326 |
A | HOH330 |
A | HOH341 |
A | HOH406 |
A | HOH409 |
A | HOH423 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue IPR B 201 |
Chain | Residue |
B | ALA11 |
B | ARG27 |
B | GLY40 |
B | GLY41 |
B | HIS42 |
B | GLU60 |
B | ASN76 |
B | LYS110 |
B | MG202 |
B | MG203 |
B | MG204 |
B | HOH340 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue MG B 202 |
Chain | Residue |
B | GLY40 |
B | GLU60 |
B | IPR201 |
B | HOH304 |
B | HOH340 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue MG B 203 |
Chain | Residue |
B | GLU56 |
B | IPR201 |
B | MG204 |
B | HOH322 |
B | HOH328 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MG B 204 |
Chain | Residue |
B | GLU56 |
B | GLU60 |
B | IPR201 |
B | MG203 |
B | HOH304 |
B | HOH317 |
Functional Information from PROSITE/UniProt
site_id | PS00893 |
Number of Residues | 22 |
Details | NUDIX_BOX Nudix box signature. GhlefgEsfeeCAaREVmEEtG |
Chain | Residue | Details |
A | GLY41-GLY62 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU56 | |
A | GLU60 | |
B | GLU56 | |
B | GLU60 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | SER2 | |
B | SER2 |