3X1J
Crystal Structure of Phosphopantetheine adenylyltransferase (PPAT/CoaD) with AcCoA from Pseudomonas aeruginosa
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0008771 | molecular_function | [citrate (pro-3S)-lyase] ligase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0015937 | biological_process | coenzyme A biosynthetic process |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0008771 | molecular_function | [citrate (pro-3S)-lyase] ligase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0015937 | biological_process | coenzyme A biosynthetic process |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
C | 0003824 | molecular_function | catalytic activity |
C | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0008771 | molecular_function | [citrate (pro-3S)-lyase] ligase activity |
C | 0009058 | biological_process | biosynthetic process |
C | 0015937 | biological_process | coenzyme A biosynthetic process |
C | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ACO A 201 |
Chain | Residue |
A | TYR6 |
A | ARG87 |
A | GLY88 |
A | ARG90 |
A | TYR97 |
A | LEU101 |
A | ASN105 |
A | SER127 |
A | SER128 |
A | THR129 |
A | DMS207 |
A | PRO7 |
A | HOH303 |
C | LEU130 |
C | ILE134 |
C | LEU137 |
A | GLY8 |
A | THR9 |
A | HIS17 |
A | ALA36 |
A | LYS41 |
A | LEU72 |
A | LEU73 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 202 |
Chain | Residue |
A | GLY68 |
A | PHE69 |
A | SER70 |
A | THR71 |
A | PHE76 |
A | GOL204 |
A | HOH319 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 203 |
Chain | Residue |
A | ASN83 |
A | ASP111 |
C | ARG26 |
C | LEU27 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 204 |
Chain | Residue |
A | LEU47 |
A | GLY68 |
A | PHE69 |
A | SER70 |
A | PO4202 |
A | GOL205 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 205 |
Chain | Residue |
A | GOL204 |
C | HIS75 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 206 |
Chain | Residue |
A | GLU48 |
A | GLN49 |
C | LEU47 |
C | GLY68 |
C | PHE69 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMS A 207 |
Chain | Residue |
A | ALA37 |
A | SER38 |
A | PRO39 |
A | PHE69 |
A | SER70 |
A | THR71 |
A | ACO201 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 208 |
Chain | Residue |
A | LYS15 |
A | GLY18 |
A | ASP19 |
A | TYR123 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PEG A 209 |
Chain | Residue |
A | GLU155 |
A | ARG156 |
A | LYS158 |
C | GLN55 |
C | GLU65 |
C | VAL66 |
C | HOH308 |
site_id | BC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ACO B 201 |
Chain | Residue |
A | GLU133 |
A | LEU137 |
B | TYR6 |
B | PRO7 |
B | GLY8 |
B | THR9 |
B | HIS17 |
B | ALA36 |
B | LYS41 |
B | PHE69 |
B | THR71 |
B | LEU72 |
B | LEU73 |
B | ARG87 |
B | GLY88 |
B | ARG90 |
B | TYR97 |
B | ASN105 |
B | SER127 |
B | SER128 |
B | THR129 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS B 202 |
Chain | Residue |
B | LYS15 |
B | GLY18 |
B | ASP19 |
B | GLU22 |
B | TYR123 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS B 203 |
Chain | Residue |
B | ARG26 |
B | LEU27 |
B | ASN83 |
B | ASP111 |
B | HOH305 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS B 204 |
Chain | Residue |
B | GLU79 |
B | GLY68 |
B | SER70 |
B | THR71 |
site_id | BC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ACO C 201 |
Chain | Residue |
B | LEU130 |
B | GLU133 |
B | ILE134 |
C | TYR6 |
C | PRO7 |
C | GLY8 |
C | THR9 |
C | HIS17 |
C | LYS41 |
C | PHE69 |
C | THR71 |
C | LEU73 |
C | ARG87 |
C | ARG90 |
C | TYR97 |
C | LEU101 |
C | ASN105 |
C | SER127 |
C | SER128 |
C | THR129 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS C 202 |
Chain | Residue |
C | LYS15 |
C | GLY18 |
C | ASP19 |
C | GLU22 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMS C 203 |
Chain | Residue |
A | PRO39 |
C | GLU133 |