5C7T
Crystal Structure of the Bdellovibrio bacteriovorus Nucleoside Diphosphate Sugar Hydrolase in complex with ADP-ribose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006753 | biological_process | nucleoside phosphate metabolic process |
| A | 0008768 | molecular_function | UDP-sugar diphosphatase activity |
| A | 0008893 | molecular_function | guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019144 | molecular_function | ADP-sugar diphosphatase activity |
| A | 0019693 | biological_process | ribose phosphate metabolic process |
| A | 0034432 | molecular_function | bis(5'-adenosyl)-pentaphosphatase activity |
| A | 0047631 | molecular_function | ADP-ribose diphosphatase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006753 | biological_process | nucleoside phosphate metabolic process |
| B | 0008768 | molecular_function | UDP-sugar diphosphatase activity |
| B | 0008893 | molecular_function | guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019144 | molecular_function | ADP-sugar diphosphatase activity |
| B | 0019693 | biological_process | ribose phosphate metabolic process |
| B | 0034432 | molecular_function | bis(5'-adenosyl)-pentaphosphatase activity |
| B | 0047631 | molecular_function | ADP-ribose diphosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue APR A 201 |
| Chain | Residue |
| A | TYR19 |
| A | HOH329 |
| A | HOH330 |
| A | HOH354 |
| A | HOH381 |
| A | HOH389 |
| B | THR36 |
| B | ARG37 |
| B | GLU38 |
| B | ILE114 |
| B | GLY115 |
| A | ARG64 |
| B | SO4201 |
| A | GLY77 |
| A | LYS78 |
| A | GLU119 |
| A | GLY139 |
| A | LYS165 |
| A | HOH309 |
| A | HOH321 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 202 |
| Chain | Residue |
| A | ARG18 |
| A | TYR19 |
| A | HOH311 |
| B | TYR35 |
| B | THR36 |
| B | HOH320 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 203 |
| Chain | Residue |
| A | ARG12 |
| A | GLN26 |
| A | ARG127 |
| A | HOH334 |
| B | PEG202 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 204 |
| Chain | Residue |
| A | LYS90 |
| A | HOH301 |
| A | HOH343 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 205 |
| Chain | Residue |
| A | ILE14 |
| A | LEU51 |
| A | ARG127 |
| A | ASP128 |
| A | HOH346 |
| A | HOH353 |
| A | HOH380 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 206 |
| Chain | Residue |
| A | LYS69 |
| A | VAL70 |
| A | PHE71 |
| A | GLY159 |
| A | LYS160 |
| A | VAL161 |
| A | SER162 |
| A | HOH314 |
| B | HIS111 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 207 |
| Chain | Residue |
| A | PRO149 |
| A | ALA150 |
| A | MET153 |
| A | ASP174 |
| A | HOH324 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue PG0 A 208 |
| Chain | Residue |
| A | HIS61 |
| A | VAL70 |
| A | HOH355 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 209 |
| Chain | Residue |
| A | THR34 |
| A | TYR35 |
| A | THR36 |
| A | GLY179 |
| B | ARG18 |
| B | TYR19 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 210 |
| Chain | Residue |
| A | ARG37 |
| A | HOH347 |
| A | HOH349 |
| A | HOH371 |
| B | TYR63 |
| B | ARG64 |
| B | APR203 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 201 |
| Chain | Residue |
| A | TYR63 |
| A | ARG64 |
| A | APR201 |
| B | ARG37 |
| B | GLY115 |
| B | HOH317 |
| B | HOH331 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue PEG B 202 |
| Chain | Residue |
| A | GLN26 |
| A | THR36 |
| A | PHE176 |
| A | LEU177 |
| A | ASN182 |
| A | SO4203 |
| A | HOH315 |
| B | ARG18 |
| site_id | AD4 |
| Number of Residues | 23 |
| Details | binding site for residue APR B 203 |
| Chain | Residue |
| B | GLU119 |
| B | GLN138 |
| B | GLY139 |
| B | GLN140 |
| B | LYS165 |
| B | GOL204 |
| B | HOH330 |
| B | HOH349 |
| B | HOH353 |
| B | HOH371 |
| A | THR36 |
| A | ARG37 |
| A | GLU38 |
| A | ILE114 |
| A | GLY115 |
| A | TYR116 |
| A | SO4210 |
| A | HOH347 |
| B | TYR19 |
| B | ARG64 |
| B | ALA76 |
| B | GLY77 |
| B | LYS78 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 204 |
| Chain | Residue |
| B | LYS78 |
| B | ASP80 |
| B | ARG91 |
| B | GLU92 |
| B | APR203 |
| B | HOH338 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 205 |
| Chain | Residue |
| B | LYS69 |
| B | VAL70 |
| B | PHE71 |
| B | LEU72 |
| B | GLY159 |
| B | LYS160 |
| B | SER162 |
| B | PGE208 |
| B | HOH343 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 206 |
| Chain | Residue |
| A | ARG18 |
| B | HIS131 |
| B | HOH319 |
| B | HOH358 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 207 |
| Chain | Residue |
| B | ASN56 |
| B | GLU146 |
| B | LYS148 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue PGE B 208 |
| Chain | Residue |
| B | HIS61 |
| B | LYS160 |
| B | GOL205 |
| B | HOH321 |
Functional Information from PROSITE/UniProt
| site_id | PS00893 |
| Number of Residues | 22 |
| Details | NUDIX_BOX Nudix box signature. GkrdhnEetllTAkRELlEEtG |
| Chain | Residue | Details |
| A | GLY77-GLY98 |
