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 EXJ A 201 |
Chain | Residue |
A | GLY9 |
A | MET105 |
A | ASN106 |
A | GLU134 |
A | HIS138 |
A | HOH310 |
A | HOH315 |
A | HOH322 |
A | ALA37 |
A | ALA38 |
A | SER39 |
A | SER71 |
A | ASP72 |
A | LEU73 |
A | MET74 |
A | LEU102 |
site_id | AC2 |
Number of Residues | 23 |
Details | binding site for residue ATP A 202 |
Chain | Residue |
A | TYR7 |
A | THR10 |
A | PHE11 |
A | GLY17 |
A | HIS18 |
A | ILE21 |
A | ARG88 |
A | GLY89 |
A | ARG91 |
A | ASP95 |
A | GLU99 |
A | PRO120 |
A | TRP124 |
A | ILE127 |
A | SER128 |
A | SER129 |
A | SER130 |
A | MG203 |
A | HOH306 |
A | HOH331 |
A | HOH348 |
A | HOH361 |
A | HOH368 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue MG A 203 |
Chain | Residue |
A | ATP202 |
A | HOH361 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 204 |
Chain | Residue |
A | SER121 |
A | LYS122 |
A | HOH301 |
A | HOH302 |
A | HOH317 |
B | HIS104 |
B | ARG107 |
site_id | AC5 |
Number of Residues | 15 |
Details | binding site for residue EXJ B 201 |
Chain | Residue |
B | GLY9 |
B | THR10 |
B | ALA37 |
B | ALA38 |
B | SER39 |
B | PHE70 |
B | SER71 |
B | ASP72 |
B | LEU73 |
B | MET74 |
B | LEU102 |
B | MET105 |
B | HOH312 |
B | HOH348 |
B | HOH371 |
site_id | AC6 |
Number of Residues | 21 |
Details | binding site for residue ATP B 202 |
Chain | Residue |
B | TYR7 |
B | PRO8 |
B | THR10 |
B | PHE11 |
B | GLY17 |
B | HIS18 |
B | ILE21 |
B | ARG88 |
B | GLY89 |
B | ARG91 |
B | PRO120 |
B | TRP124 |
B | ILE127 |
B | SER128 |
B | SER129 |
B | SER130 |
B | MG203 |
B | HOH308 |
B | HOH330 |
B | HOH339 |
B | HOH347 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue MG B 203 |
Chain | Residue |
B | ATP202 |
B | HOH400 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 204 |
Chain | Residue |
A | HIS104 |
A | ARG107 |
B | SER121 |
B | LYS122 |
B | HOH304 |
B | HOH305 |
B | HOH311 |
B | HOH333 |
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 |