Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004747 | molecular_function | ribokinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006014 | biological_process | D-ribose metabolic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0019303 | biological_process | D-ribose catabolic process |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046835 | biological_process | carbohydrate phosphorylation |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AB1 |
Number of Residues | 4 |
Details | RESIDUES MAKING DIRECT HYDROGEN BONDS WITH ADP. |
Chain | Residue |
A | ASN187 |
A | THR223 |
A | GLY225 |
A | ALA280 |
site_id | AB2 |
Number of Residues | 7 |
Details | RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP. |
Chain | Residue |
A | ASN166 |
A | ASN187 |
A | GLU190 |
A | THR223 |
A | PHE243 |
A | VAL245 |
A | ALA280 |
site_id | AB3 |
Number of Residues | 5 |
Details | RESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP. |
Chain | Residue |
A | GLY225 |
A | VAL245 |
A | ALA253 |
A | ALA282 |
A | VAL286 |
site_id | RB1 |
Number of Residues | 7 |
Details | RESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE. |
Chain | Residue |
A | ASN14 |
A | ASP16 |
A | GLY42 |
A | LYS43 |
A | ASN46 |
A | GLU143 |
A | ASP255 |
site_id | RB2 |
Number of Residues | 3 |
Details | RESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH RIBOSE. |
Chain | Residue |
A | ASP255 |
A | ALA252 |
A | GLY254 |
site_id | RB3 |
Number of Residues | 5 |
Details | RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE. |
Chain | Residue |
A | ALA98 |
A | ILE100 |
A | ILE110 |
A | ILE112 |
A | ILE251 |
Functional Information from PROSITE/UniProt
site_id | PS00584 |
Number of Residues | 14 |
Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTiAAGDtfnGALI |
Chain | Residue | Details |
A | ASP249-ILE262 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP255 | |
Chain | Residue | Details |
A | ASN14 | |
A | GLY42 | |
A | GLU143 | |
A | ASN187 | |
A | THR223 | |
A | ASP255 | |
A | HIS279 | |
Chain | Residue | Details |
A | ASP249 | |
A | ILE251 | |
A | ALA285 | |
A | ARG288 | |
A | GLY290 | |
A | SER294 | |
Chain | Residue | Details |
A | GLY254 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
A | GLY254 | |
A | ASP255 | |
A | ALA253 | |
A | ALA252 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 663 |
Chain | Residue | Details |
A | ALA252 | electrostatic stabiliser, polar interaction |
A | ALA253 | electrostatic stabiliser, polar interaction |
A | GLY254 | electrostatic stabiliser, polar interaction |
A | ASP255 | electrostatic stabiliser, proton acceptor, proton donor |