3H49
Crystal structure of a putative Ribokinase (Apo Form) from E.coli at 1.8A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006796 | biological_process | phosphate-containing compound metabolic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0019200 | molecular_function | carbohydrate kinase activity |
| A | 0019698 | biological_process | D-galacturonate catabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042840 | biological_process | D-glucuronate catabolic process |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0005829 | cellular_component | cytosol |
| B | 0006796 | biological_process | phosphate-containing compound metabolic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0019200 | molecular_function | carbohydrate kinase activity |
| B | 0019698 | biological_process | D-galacturonate catabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042840 | biological_process | D-glucuronate catabolic process |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00583 |
| Number of Residues | 25 |
| Details | PFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGdAiNEAtiIsRLGhrtalmsriG |
| Chain | Residue | Details |
| A | GLY41-GLY65 |
| site_id | PS00584 |
| Number of Residues | 14 |
| Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTiGAGDnfaSGFI |
| Chain | Residue | Details |
| A | ASP254-ILE267 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | ASP260 | |
| A | ARG108 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | ASP260 | |
| B | ARG108 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | GLY259 | |
| A | GLY257 | |
| A | ALA258 | |
| A | ASP260 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | GLY259 | |
| B | GLY257 | |
| B | ALA258 | |
| B | ASP260 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | GLY257 | |
| A | LYS227 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | GLY257 | |
| B | LYS227 |
