5JBN
Crystal Structure of Apo Phosphopantetheine Adenylyltransferase (PPAT/CoaD) from E. coli
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 | 7 |
| Details | binding site for residue SO4 A 201 |
| Chain | Residue |
| A | SER121 |
| A | LYS122 |
| A | HOH309 |
| A | HOH312 |
| A | HOH356 |
| B | HIS104 |
| B | ARG107 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 202 |
| Chain | Residue |
| A | SER129 |
| A | HOH316 |
| A | HOH319 |
| A | HIS18 |
| A | ARG91 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 203 |
| Chain | Residue |
| A | ALA37 |
| A | PHE70 |
| A | ASP72 |
| A | LEU73 |
| A | MET74 |
| A | GLU134 |
| A | HIS138 |
| A | HOH393 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue DMS A 204 |
| Chain | Residue |
| A | HIS108 |
| A | ASP141 |
| A | HIS144 |
| A | HOH310 |
| A | HOH352 |
| A | HOH377 |
| B | HIS82 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 201 |
| Chain | Residue |
| A | ARG107 |
| B | SER121 |
| B | LYS122 |
| B | HOH302 |
| B | HOH316 |
| B | HOH322 |
| B | HOH335 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 202 |
| Chain | Residue |
| B | SER39 |
| B | PRO40 |
| B | SER41 |
| B | ARG137 |
| B | HIS138 |
| B | HOH309 |
| B | HOH402 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 203 |
| Chain | Residue |
| B | HIS18 |
| B | SER128 |
| B | SER129 |
| B | HOH307 |
| B | HOH344 |
| B | HOH422 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11812124","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GN8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11812124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12837781","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QJC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11812124","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QJC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"11812124","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
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 |
