Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006000 | biological_process | fructose metabolic process |
A | 0008865 | molecular_function | fructokinase activity |
A | 0016301 | molecular_function | kinase activity |
A | 0046835 | biological_process | carbohydrate phosphorylation |
A | 0046872 | molecular_function | metal ion binding |
B | 0005524 | molecular_function | ATP binding |
B | 0006000 | biological_process | fructose metabolic process |
B | 0008865 | molecular_function | fructokinase activity |
B | 0016301 | molecular_function | kinase activity |
B | 0046835 | biological_process | carbohydrate phosphorylation |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 404 |
Chain | Residue |
A | ASP246 |
A | THR248 |
A | ALA287 |
A | ALA290 |
A | GLY292 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K A 405 |
Chain | Residue |
A | ALA180 |
A | ALA181 |
A | ALA183 |
A | GLY213 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K B 406 |
Chain | Residue |
B | ALA180 |
B | ALA181 |
B | ALA183 |
B | GLY213 |
B | HOH603 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K B 407 |
Chain | Residue |
B | ASP246 |
B | THR248 |
B | ALA287 |
B | ALA290 |
B | GLY292 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AIS A 402 |
Chain | Residue |
A | ASP12 |
A | SER14 |
A | ASP16 |
A | GLY31 |
A | ASN35 |
A | LEU87 |
A | PHE99 |
A | TYR101 |
A | ARG162 |
A | MSE165 |
A | ASP252 |
A | ALA293 |
A | HOH601 |
Functional Information from PROSITE/UniProt
site_id | PS00584 |
Number of Residues | 14 |
Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDafvGGLL |
Chain | Residue | Details |
A | ASP246-LEU259 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP252 | |
B | ASP252 | |
Chain | Residue | Details |
A | ASP16 | |
B | ASP252 | |
B | ALA290 | |
B | GLY292 | |
A | GLY31 | |
A | ARG162 | |
A | ASP252 | |
A | ALA290 | |
A | GLY292 | |
B | ASP16 | |
B | GLY31 | |
B | ARG162 | |
Chain | Residue | Details |
A | TYR101 | |
B | TYR101 | |
Chain | Residue | Details |
A | ASP158 | |
B | ASN281 | |
A | LYS187 | |
A | GLU192 | |
A | SER220 | |
A | ASN281 | |
B | ASP158 | |
B | LYS187 | |
B | GLU192 | |
B | SER220 | |
Chain | Residue | Details |
A | ALA180 | |
B | ALA183 | |
B | GLY213 | |
B | ASP246 | |
B | THR248 | |
B | ALA287 | |
A | ALA181 | |
A | ALA183 | |
A | GLY213 | |
A | ASP246 | |
A | THR248 | |
A | ALA287 | |
B | ALA180 | |
B | ALA181 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 15458630 |
Chain | Residue | Details |
A | GLY249 | |
A | GLY251 | |
A | ASP252 | |
A | ASP252 | |
A | ALA250 | |
site_id | CSA2 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 15458630 |
Chain | Residue | Details |
B | GLY249 | |
B | GLY251 | |
B | ASP252 | |
B | ASP252 | |
B | ALA250 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 751 |
Chain | Residue | Details |
A | GLY249 | electrostatic stabiliser |
A | ALA250 | electrostatic stabiliser |
A | GLY251 | electrostatic stabiliser |
A | ASP252 | electrostatic stabiliser, proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 751 |
Chain | Residue | Details |
B | GLY249 | electrostatic stabiliser |
B | ALA250 | electrostatic stabiliser |
B | GLY251 | electrostatic stabiliser |
B | ASP252 | electrostatic stabiliser, proton shuttle (general acid/base) |