1WYE
Crystal structure of 2-keto-3-deoxygluconate kinase (form 1) from Sulfolobus Tokodaii
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0046835 | biological_process | carbohydrate phosphorylation |
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 | 0046835 | biological_process | carbohydrate phosphorylation |
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 | 0046835 | biological_process | carbohydrate phosphorylation |
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 | 0046835 | biological_process | carbohydrate phosphorylation |
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 | 0046835 | biological_process | carbohydrate phosphorylation |
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 | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q97U29 |
Chain | Residue | Details |
A | ASP256 | |
B | ASP256 | |
C | ASP256 | |
D | ASP256 | |
E | ASP256 | |
F | ASP256 |
site_id | SWS_FT_FI2 |
Number of Residues | 48 |
Details | BINDING: BINDING => ECO:0000305|Ref.4 |
Chain | Residue | Details |
A | GLY34 | |
B | TYR106 | |
B | ARG166 | |
B | LYS224 | |
B | GLY253 | |
B | ASP256 | |
B | SER283 | |
B | ASP292 | |
C | GLY34 | |
C | TYR106 | |
C | ARG166 | |
A | TYR106 | |
C | LYS224 | |
C | GLY253 | |
C | ASP256 | |
C | SER283 | |
C | ASP292 | |
D | GLY34 | |
D | TYR106 | |
D | ARG166 | |
D | LYS224 | |
D | GLY253 | |
A | ARG166 | |
D | ASP256 | |
D | SER283 | |
D | ASP292 | |
E | GLY34 | |
E | TYR106 | |
E | ARG166 | |
E | LYS224 | |
E | GLY253 | |
E | ASP256 | |
E | SER283 | |
A | LYS224 | |
E | ASP292 | |
F | GLY34 | |
F | TYR106 | |
F | ARG166 | |
F | LYS224 | |
F | GLY253 | |
F | ASP256 | |
F | SER283 | |
F | ASP292 | |
A | GLY253 | |
A | ASP256 | |
A | SER283 | |
A | ASP292 | |
B | GLY34 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q97U29 |
Chain | Residue | Details |
A | ASN164 | |
B | ASN164 | |
C | ASN164 | |
D | ASN164 | |
E | ASN164 | |
F | ASN164 |
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 |