2VAR
Crystal structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase complexed with 2-keto-3-deoxygluconate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005524 | molecular_function | ATP binding |
A | 0008671 | molecular_function | 2-dehydro-3-deoxygalactonokinase activity |
A | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016740 | molecular_function | transferase activity |
A | 0046835 | biological_process | carbohydrate phosphorylation |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005524 | molecular_function | ATP binding |
B | 0008671 | molecular_function | 2-dehydro-3-deoxygalactonokinase activity |
B | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0016740 | molecular_function | transferase activity |
B | 0046835 | biological_process | carbohydrate phosphorylation |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005524 | molecular_function | ATP binding |
C | 0008671 | molecular_function | 2-dehydro-3-deoxygalactonokinase activity |
C | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
C | 0016301 | molecular_function | kinase activity |
C | 0016310 | biological_process | phosphorylation |
C | 0016740 | molecular_function | transferase activity |
C | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19018105","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 60 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19018105","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
A | GLY257 | |
A | GLY255 | |
A | ASP258 | |
A | ALA256 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
B | GLY257 | |
B | GLY255 | |
B | ASP258 | |
B | ALA256 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
C | GLY257 | |
C | GLY255 | |
C | ASP258 | |
C | ALA256 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
A | LYS226 | |
A | GLY255 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
B | LYS226 | |
B | GLY255 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
C | LYS226 | |
C | GLY255 |