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 | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 603 |
Chain | Residue |
A | SER121 |
A | LYS122 |
A | HOH2113 |
A | HOH2114 |
B | HIS104 |
B | ARG107 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MN A 802 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 601 |
Chain | Residue |
B | SER41 |
B | ARG137 |
B | HIS138 |
B | HOH2031 |
B | SER39 |
B | PRO40 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 602 |
Chain | Residue |
A | HIS104 |
A | ARG107 |
B | SER121 |
B | LYS122 |
B | HOH2128 |
B | HOH2129 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MN B 801 |
site_id | AC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ATP A 700 |
Chain | Residue |
A | TYR7 |
A | THR10 |
A | PHE11 |
A | GLY17 |
A | HIS18 |
A | ILE21 |
A | ARG88 |
A | GLY89 |
A | ARG91 |
A | PRO120 |
A | TRP124 |
A | ILE127 |
A | SER128 |
A | SER129 |
A | SER130 |
A | MN802 |
A | HOH2011 |
A | HOH2063 |
A | HOH2089 |
A | HOH2115 |
A | HOH2116 |
A | HOH2117 |
A | HOH2118 |
site_id | AC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ATP B 600 |
Chain | Residue |
B | TYR7 |
B | THR10 |
B | PHE11 |
B | GLY17 |
B | HIS18 |
B | ILE21 |
B | ARG88 |
B | GLY89 |
B | ARG91 |
B | GLU99 |
B | PRO120 |
B | TRP124 |
B | ILE127 |
B | SER128 |
B | SER129 |
B | SER130 |
B | MN801 |
B | HOH2013 |
B | HOH2104 |
B | HOH2126 |
B | HOH2127 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR10 | |
A | LYS42 | |
A | MET74 | |
B | THR10 | |
B | LYS42 | |
B | MET74 | |
Chain | Residue | Details |
A | HIS18 | |
B | TYR7 | |
A | GLY89 | |
A | GLU99 | |
A | TRP124 | |
B | HIS18 | |
B | GLY89 | |
B | GLU99 | |
B | TRP124 | |
A | TYR7 | |
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 |