1ESM
STRUCTURAL BASIS FOR THE FEEDBACK REGULATION OF ESCHERICHIA COLI PANTOTHENATE KINASE BY COENZYME A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004594 | molecular_function | pantothenate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050165 | molecular_function | pantetheine kinase activity |
| B | 0004594 | molecular_function | pantothenate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0015937 | biological_process | coenzyme A biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050165 | molecular_function | pantetheine kinase activity |
| C | 0004594 | molecular_function | pantothenate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0015937 | biological_process | coenzyme A biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0050165 | molecular_function | pantetheine kinase activity |
| D | 0004594 | molecular_function | pantothenate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0015937 | biological_process | coenzyme A biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0050165 | molecular_function | pantetheine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE COA A 401 |
| Chain | Residue |
| A | GLY41 |
| A | HIS177 |
| A | TYR180 |
| A | LEU201 |
| A | TYR240 |
| A | ARG243 |
| A | PHE247 |
| A | PHE252 |
| A | ASN282 |
| C | ARG38 |
| A | ILE42 |
| A | VAL97 |
| A | ALA98 |
| A | LYS101 |
| A | SER102 |
| A | ARG106 |
| A | LYS145 |
| A | TYR175 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE COA C 402 |
| Chain | Residue |
| A | ARG38 |
| C | GLY41 |
| C | ILE42 |
| C | VAL97 |
| C | ALA98 |
| C | LYS101 |
| C | SER102 |
| C | ARG106 |
| C | LYS145 |
| C | HIS177 |
| C | TYR180 |
| C | LEU201 |
| C | TYR240 |
| C | ARG243 |
| C | PHE247 |
| C | PHE252 |
| C | ASN282 |
| C | HOH577 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE COA D 403 |
| Chain | Residue |
| B | ARG38 |
| D | GLY41 |
| D | ILE42 |
| D | VAL97 |
| D | ALA98 |
| D | LYS101 |
| D | SER102 |
| D | ARG106 |
| D | LYS145 |
| D | TYR175 |
| D | HIS177 |
| D | TYR180 |
| D | LEU201 |
| D | TYR240 |
| D | ARG243 |
| D | PHE247 |
| D | PHE252 |
| D | ASN282 |
| D | HOH515 |
| D | HOH772 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE COA B 404 |
| Chain | Residue |
| B | GLY41 |
| B | ILE42 |
| B | VAL97 |
| B | ALA98 |
| B | LYS101 |
| B | SER102 |
| B | ARG106 |
| B | LYS145 |
| B | TYR175 |
| B | HIS177 |
| B | TYR180 |
| B | LEU201 |
| B | TYR240 |
| B | ARG243 |
| B | PHE247 |
| B | PHE252 |
| B | ASN282 |
| B | HOH799 |
| B | HOH803 |
| B | HOH805 |
| D | ARG38 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY95 | |
| B | GLY95 | |
| C | GLY95 | |
| D | GLY95 |
