4BC2
Crystal structure of human D-xylulokinase in complex with D-xylulose and adenosine diphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004856 | molecular_function | D-xylulokinase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005997 | biological_process | xylulose metabolic process |
| A | 0005998 | biological_process | xylulose catabolic process |
| A | 0006091 | biological_process | generation of precursor metabolites and energy |
| A | 0016301 | molecular_function | kinase activity |
| A | 0019640 | biological_process | obsolete D-glucuronate catabolic process to D-xylulose 5-phosphate |
| A | 0042732 | biological_process | D-xylose metabolic process |
| B | 0004856 | molecular_function | D-xylulokinase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005997 | biological_process | xylulose metabolic process |
| B | 0005998 | biological_process | xylulose catabolic process |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0016301 | molecular_function | kinase activity |
| B | 0019640 | biological_process | obsolete D-glucuronate catabolic process to D-xylulose 5-phosphate |
| B | 0042732 | biological_process | D-xylose metabolic process |
| C | 0004856 | molecular_function | D-xylulokinase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0005997 | biological_process | xylulose metabolic process |
| C | 0005998 | biological_process | xylulose catabolic process |
| C | 0006091 | biological_process | generation of precursor metabolites and energy |
| C | 0016301 | molecular_function | kinase activity |
| C | 0019640 | biological_process | obsolete D-glucuronate catabolic process to D-xylulose 5-phosphate |
| C | 0042732 | biological_process | D-xylose metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ADP B 1533 |
| Chain | Residue |
| B | SER340 |
| B | TRP355 |
| B | GLY441 |
| B | ALA442 |
| B | ASN445 |
| B | HOH2178 |
| B | HOH2180 |
| B | HOH2284 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ADP A 1533 |
| Chain | Residue |
| A | GLY441 |
| A | ASN445 |
| A | HOH2183 |
| A | HOH2184 |
| A | HOH2237 |
| A | TRP355 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP C 1533 |
| Chain | Residue |
| A | HOH2040 |
| C | LEU299 |
| C | SER340 |
| C | GLU344 |
| C | TRP355 |
| C | GLY441 |
| C | ALA442 |
| C | ASN445 |
| C | HOH2138 |
| C | HOH2151 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE XUL B 1534 |
| Chain | Residue |
| B | GLN97 |
| B | GLN98 |
| B | HIS99 |
| B | TRP137 |
| B | ARG170 |
| B | ASP280 |
| B | ASN281 |
| B | HOH2015 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE XUL C 1534 |
| Chain | Residue |
| C | GLN97 |
| C | GLN98 |
| C | HIS99 |
| C | TRP137 |
| C | ARG170 |
| C | ASP280 |
| C | ASN281 |
| C | HOH2011 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE XUL A 1534 |
| Chain | Residue |
| A | GLN97 |
| A | GLN98 |
| A | HIS99 |
| A | TRP137 |
| A | ARG170 |
| A | ASP280 |
| A | ASN281 |
| A | HOH2009 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1535 |
| Chain | Residue |
| B | SER251 |
| B | CYS252 |
| B | PRO324 |
| B | VAL325 |
| B | ASP326 |
| B | SER327 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | Binding site: {} |
| Chain | Residue | Details |
