1V1S
2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS (CRYSTAL FORM 2)
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 | 0016310 | biological_process | phosphorylation |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| 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 | 0016310 | biological_process | phosphorylation |
| B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| 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 | 0016310 | biological_process | phosphorylation |
| C | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| 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 | 0016310 | biological_process | phosphorylation |
| D | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| 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 | 0016310 | biological_process | phosphorylation |
| E | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| 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 | 0016310 | biological_process | phosphorylation |
| F | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| F | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00584 |
| Number of Residues | 14 |
| Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DPvGAGDafaAGYL |
| Chain | Residue | Details |
| A | ASP245-LEU258 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:15210349 |
| Chain | Residue | Details |
| A | ASP251 | |
| B | ASP251 | |
| C | ASP251 | |
| D | ASP251 | |
| E | ASP251 | |
| F | ASP251 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 54 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15210349 |
| Chain | Residue | Details |
| A | GLY34 | |
| B | GLY34 | |
| B | TYR103 | |
| B | ARG167 | |
| B | SER193 | |
| B | LYS219 | |
| B | GLY248 | |
| B | ASP251 | |
| B | ASN275 | |
| B | ASP287 | |
| C | GLY34 | |
| A | TYR103 | |
| C | TYR103 | |
| C | ARG167 | |
| C | SER193 | |
| C | LYS219 | |
| C | GLY248 | |
| C | ASP251 | |
| C | ASN275 | |
| C | ASP287 | |
| D | GLY34 | |
| D | TYR103 | |
| A | ARG167 | |
| D | ARG167 | |
| D | SER193 | |
| D | LYS219 | |
| D | GLY248 | |
| D | ASP251 | |
| D | ASN275 | |
| D | ASP287 | |
| E | GLY34 | |
| E | TYR103 | |
| E | ARG167 | |
| A | SER193 | |
| E | SER193 | |
| E | LYS219 | |
| E | GLY248 | |
| E | ASP251 | |
| E | ASN275 | |
| E | ASP287 | |
| F | GLY34 | |
| F | TYR103 | |
| F | ARG167 | |
| F | SER193 | |
| A | LYS219 | |
| F | LYS219 | |
| F | GLY248 | |
| F | ASP251 | |
| F | ASN275 | |
| F | ASP287 | |
| A | GLY248 | |
| A | ASP251 | |
| A | ASN275 | |
| A | ASP287 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q97U29 |
| Chain | Residue | Details |
| A | TYR89 | |
| E | ASN165 | |
| F | TYR89 | |
| F | ASN165 | |
| A | ASN165 | |
| B | TYR89 | |
| B | ASN165 | |
| C | TYR89 | |
| C | ASN165 | |
| D | TYR89 | |
| D | ASN165 | |
| E | TYR89 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | GLY248 | |
| A | ALA249 | |
| A | ASP251 | |
| A | GLY250 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| D | GLY248 | |
| D | LYS219 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| E | GLY248 | |
| E | LYS219 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| F | GLY248 | |
| F | LYS219 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | ARG100 | |
| A | ASP251 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | ARG100 | |
| B | ASP251 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| C | ARG100 | |
| C | ASP251 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| D | ARG100 | |
| D | ASP251 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| E | ARG100 | |
| E | ASP251 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| F | ARG100 | |
| F | ASP251 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | GLY248 | |
| B | ALA249 | |
| B | ASP251 | |
| B | GLY250 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| C | GLY248 | |
| C | ALA249 | |
| C | ASP251 | |
| C | GLY250 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| D | GLY248 | |
| D | ALA249 | |
| D | ASP251 | |
| D | GLY250 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| E | GLY248 | |
| E | ALA249 | |
| E | ASP251 | |
| E | GLY250 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| F | GLY248 | |
| F | ALA249 | |
| F | ASP251 | |
| F | GLY250 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | GLY248 | |
| A | LYS219 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | GLY248 | |
| B | LYS219 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| C | GLY248 | |
| C | LYS219 |
