Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
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 | 0016740 | molecular_function | transferase activity |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0042802 | molecular_function | identical protein binding |
B | 0000166 | molecular_function | nucleotide 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 | 0016740 | molecular_function | transferase activity |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue F0V A 201 |
Chain | Residue |
A | GLY9 |
A | LEU131 |
A | HOH303 |
A | HOH361 |
A | THR10 |
A | PHE70 |
A | LEU73 |
A | MET74 |
A | TYR98 |
A | LEU102 |
A | MET105 |
A | ASN106 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 202 |
Chain | Residue |
A | SER121 |
A | LYS122 |
A | HOH301 |
A | HOH307 |
A | HOH314 |
B | HIS104 |
B | ARG107 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue DMS A 203 |
Chain | Residue |
A | THR26 |
A | GLN27 |
A | PHE29 |
A | ASP30 |
A | HOH351 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue PG4 A 204 |
Chain | Residue |
A | ASN16 |
A | ASP20 |
A | THR23 |
A | GLN27 |
A | TRP124 |
A | HOH323 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 205 |
Chain | Residue |
A | HIS18 |
A | ARG91 |
A | SER128 |
A | SER129 |
A | HOH350 |
A | HOH360 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 201 |
Chain | Residue |
A | HIS104 |
A | ARG107 |
B | SER121 |
B | LYS122 |
B | HOH301 |
B | HOH304 |
B | HOH307 |
B | HOH310 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 202 |
Chain | Residue |
B | SER39 |
B | PRO40 |
B | SER41 |
B | ARG137 |
B | HIS138 |
B | HOH352 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue PG4 B 203 |
Chain | Residue |
B | ALA37 |
B | ASP72 |
B | MET74 |
B | ARG88 |
B | ASN106 |
B | GLU134 |
B | VAL135 |
B | HIS138 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue DMS B 204 |
Chain | Residue |
B | TYR7 |
B | PRO8 |
B | ARG88 |
B | GLY89 |
B | SO4205 |
B | HOH308 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 205 |
Chain | Residue |
B | HIS18 |
B | ARG91 |
B | SER128 |
B | SER129 |
B | DMS204 |
B | HOH305 |
B | HOH317 |
B | HOH331 |
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 |