Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0015937 | biological_process | coenzyme A biosynthetic process |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue EX7 A 201 |
| Chain | Residue |
| A | GLY9 |
| A | ASN106 |
| A | LEU109 |
| A | GLU134 |
| A | VAL135 |
| A | HIS138 |
| A | SO4205 |
| A | HOH361 |
| A | ALA37 |
| A | SER39 |
| A | ASP72 |
| A | LEU73 |
| A | MET74 |
| A | ALA75 |
| A | LEU102 |
| A | MET105 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 202 |
| Chain | Residue |
| A | SER121 |
| A | LYS122 |
| A | HOH302 |
| A | HOH303 |
| A | HOH313 |
| B | HIS104 |
| B | ARG107 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 203 |
| Chain | Residue |
| A | HIS18 |
| A | ARG91 |
| A | SER128 |
| A | SER129 |
| A | HOH301 |
| A | HOH304 |
| A | HOH310 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 204 |
| Chain | Residue |
| A | SER39 |
| A | PRO40 |
| A | SER41 |
| A | ARG137 |
| A | HIS138 |
| A | HOH329 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 205 |
| Chain | Residue |
| A | GLY9 |
| A | THR10 |
| A | LYS42 |
| A | ARG88 |
| A | EX7201 |
| A | HOH301 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue EX7 B 201 |
| Chain | Residue |
| B | GLY9 |
| B | ALA37 |
| B | ASP72 |
| B | LEU73 |
| B | MET74 |
| B | ALA75 |
| B | LEU102 |
| B | MET105 |
| B | ASN106 |
| B | LEU109 |
| B | GLU134 |
| B | VAL135 |
| B | HIS138 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 202 |
| Chain | Residue |
| A | HIS104 |
| A | ARG107 |
| B | SER121 |
| B | LYS122 |
| B | HOH301 |
| B | HOH303 |
| B | HOH324 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 203 |
| Chain | Residue |
| B | HIS18 |
| B | SER128 |
| B | SER129 |
| B | HOH317 |
| B | HOH379 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | TYR7 | |
| B | TRP124 | |
| A | HIS18 | |
| A | GLY89 | |
| A | GLU99 | |
| A | TRP124 | |
| B | TYR7 | |
| B | HIS18 | |
| B | GLY89 | |
| B | GLU99 | |
| Chain | Residue | Details |
| A | THR10 | |
| A | LYS42 | |
| A | MET74 | |
| B | THR10 | |
| B | LYS42 | |
| B | MET74 | |
| Chain | Residue | Details |
| A | ARG88 | |
| B | ARG88 | |
| Chain | Residue | Details |
| A | HIS18 | |
| B | HIS18 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 299 |
| Chain | Residue | Details |
| A | HIS18 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS42 | attractive charge-charge interaction, electrostatic stabiliser |
| A | ARG91 | attractive charge-charge interaction, electrostatic stabiliser |
| A | SER129 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 299 |
| Chain | Residue | Details |
| B | HIS18 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS42 | attractive charge-charge interaction, electrostatic stabiliser |
| B | ARG91 | attractive charge-charge interaction, electrostatic stabiliser |
| B | SER129 | electrostatic stabiliser, hydrogen bond donor |
