1WYE
Crystal structure of 2-keto-3-deoxygluconate kinase (form 1) from Sulfolobus Tokodaii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| A | 0016301 | molecular_function | kinase activity |
| 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 | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| B | 0016301 | molecular_function | kinase activity |
| 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 | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046835 | biological_process | carbohydrate phosphorylation |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0046835 | biological_process | carbohydrate phosphorylation |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| E | 0016301 | molecular_function | kinase activity |
| E | 0016740 | molecular_function | transferase activity |
| E | 0046835 | biological_process | carbohydrate phosphorylation |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0008673 | molecular_function | 2-dehydro-3-deoxygluconokinase activity |
| F | 0016301 | molecular_function | kinase activity |
| F | 0016740 | molecular_function | transferase activity |
| F | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q97U29","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 78 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of 2-keto-3-deoxygluconate kinase from Sulfolobus tokodaii complexed with 2-keto-6-phosphogluconate.","authors":["Okazaki S.","Onda H.","Suzuki A.","Kuramitsu S.","Masui R.","Yamane T."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q97U29","evidenceCode":"ECO:0000250"}]} |
| 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 | ALA254 | |
| A | GLY255 | |
| A | GLY253 | |
| A | ASP256 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| D | LYS224 | |
| D | GLY253 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| E | LYS224 | |
| E | GLY253 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| F | LYS224 | |
| F | GLY253 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| B | ALA254 | |
| B | GLY255 | |
| B | GLY253 | |
| B | ASP256 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| C | ALA254 | |
| C | GLY255 | |
| C | GLY253 | |
| C | ASP256 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| D | ALA254 | |
| D | GLY255 | |
| D | GLY253 | |
| D | ASP256 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| E | ALA254 | |
| E | GLY255 | |
| E | GLY253 | |
| E | ASP256 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| F | ALA254 | |
| F | GLY255 | |
| F | GLY253 | |
| F | ASP256 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| A | LYS224 | |
| A | GLY253 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| B | LYS224 | |
| B | GLY253 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| C | LYS224 | |
| C | GLY253 |
