4RUK
crystal structure of Phosphoapantetheine adenylyltransferase PPAT/CoaD with CoA and pyrophosphate 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 |
D | 0003824 | molecular_function | catalytic activity |
D | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0008771 | molecular_function | [citrate (pro-3S)-lyase] ligase activity |
D | 0009058 | biological_process | biosynthetic process |
D | 0015937 | biological_process | coenzyme A biosynthetic process |
D | 0016779 | molecular_function | nucleotidyltransferase activity |
E | 0003824 | molecular_function | catalytic activity |
E | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0008771 | molecular_function | [citrate (pro-3S)-lyase] ligase activity |
E | 0009058 | biological_process | biosynthetic process |
E | 0015937 | biological_process | coenzyme A biosynthetic process |
E | 0016779 | molecular_function | nucleotidyltransferase activity |
F | 0003824 | molecular_function | catalytic activity |
F | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0008771 | molecular_function | [citrate (pro-3S)-lyase] ligase activity |
F | 0009058 | biological_process | biosynthetic process |
F | 0015937 | biological_process | coenzyme A biosynthetic process |
F | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE COA A 201 |
Chain | Residue |
A | PRO7 |
A | TYR97 |
A | LEU101 |
A | SER127 |
A | SER128 |
A | THR129 |
A | ARG132 |
A | DMS204 |
A | DMS205 |
A | ACT208 |
A | HOH320 |
A | GLY8 |
A | HOH321 |
F | LEU130 |
F | GLU133 |
A | THR9 |
A | HIS17 |
A | LYS41 |
A | LEU72 |
A | LEU73 |
A | ARG87 |
A | ARG90 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS A 202 |
Chain | Residue |
A | LYS15 |
A | ASP19 |
A | TYR123 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 203 |
Chain | Residue |
A | ALA135 |
A | GLY138 |
A | GLY139 |
A | ASP140 |
A | ILE141 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DMS A 204 |
Chain | Residue |
A | ALA36 |
A | ALA37 |
A | SER38 |
A | PHE69 |
A | THR71 |
A | COA201 |
A | HOH317 |
F | LEU137 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 205 |
Chain | Residue |
A | GLY16 |
A | ARG90 |
A | COA201 |
A | ACT208 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT A 206 |
Chain | Residue |
A | ASP140 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 208 |
Chain | Residue |
A | TYR6 |
A | PRO7 |
A | ARG87 |
A | GLY88 |
A | COA201 |
A | DMS205 |
site_id | AC8 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE COA B 201 |
Chain | Residue |
B | PRO7 |
B | GLY8 |
B | THR9 |
B | HIS17 |
B | ALA36 |
B | LYS41 |
B | PHE69 |
B | THR71 |
B | LEU72 |
B | LEU73 |
B | ARG87 |
B | TYR97 |
B | LEU101 |
B | SER127 |
B | SER128 |
B | THR129 |
B | ARG132 |
B | HOH306 |
E | GLU133 |
E | LEU137 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT B 202 |
Chain | Residue |
B | SER25 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT B 204 |
Chain | Residue |
B | VAL67 |
B | GLY68 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT B 205 |
Chain | Residue |
B | GLN55 |
B | GLU65 |
B | VAL66 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT B 206 |
Chain | Residue |
B | GLU65 |
B | VAL67 |
B | GLN80 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT B 207 |
Chain | Residue |
B | ASP140 |
B | ILE141 |
B | SER142 |
B | LYS143 |
B | PHE144 |
site_id | BC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE COA C 201 |
Chain | Residue |
A | LEU130 |
A | GLU133 |
A | LEU137 |
C | GLY8 |
C | THR9 |
C | LYS41 |
C | PHE69 |
C | LEU72 |
C | LEU73 |
C | ARG87 |
C | TYR97 |
C | LEU101 |
C | SER127 |
C | SER128 |
C | THR129 |
C | HOH305 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT C 202 |
Chain | Residue |
C | LYS81 |
C | ALA82 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT C 203 |
Chain | Residue |
C | LYS15 |
C | GLY18 |
C | ASP19 |
C | HOH317 |
site_id | BC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT C 204 |
Chain | Residue |
C | GLU65 |
C | GLN80 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT C 205 |
Chain | Residue |
C | ASN83 |
C | ASP111 |
D | ARG26 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT C 206 |
Chain | Residue |
C | TYR6 |
C | HIS17 |
C | ARG87 |
C | GLY88 |
C | ARG90 |
site_id | CC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE COA D 201 |
Chain | Residue |
B | GLU133 |
B | LEU137 |
D | PRO7 |
D | GLY8 |
D | THR9 |
D | LYS41 |
D | LEU72 |
D | LEU73 |
D | ARG87 |
D | ARG90 |
D | SER93 |
D | ASP94 |
D | TYR97 |
D | LEU101 |
D | SER127 |
D | SER128 |
D | THR129 |
D | DMS203 |
D | HOH318 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE POP D 202 |
Chain | Residue |
D | TYR6 |
D | HIS17 |
D | LEU20 |
D | ARG87 |
D | GLY88 |
D | ARG90 |
site_id | CC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DMS D 203 |
Chain | Residue |
B | LEU137 |
D | ALA36 |
D | ALA37 |
D | SER38 |
D | PHE69 |
D | SER70 |
D | THR71 |
D | COA201 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS D 204 |
Chain | Residue |
D | GLY68 |
D | PHE69 |
D | SER70 |
D | THR71 |
D | FMT205 |
site_id | CC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT D 205 |
Chain | Residue |
D | DMS204 |
site_id | CC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL D 206 |
Chain | Residue |
D | LYS40 |
D | LYS41 |
site_id | CC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT E 201 |
Chain | Residue |
E | ARG132 |
site_id | CC9 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE COA E 202 |
Chain | Residue |
D | LEU130 |
D | ILE134 |
D | LEU137 |
E | PRO7 |
E | GLY8 |
E | THR9 |
E | PHE10 |
E | HIS17 |
E | ALA36 |
E | SER38 |
E | LYS41 |
E | PHE69 |
E | SER70 |
E | THR71 |
E | LEU73 |
E | ARG87 |
E | TYR97 |
E | LEU101 |
E | SER127 |
E | SER128 |
E | THR129 |
E | CA203 |
E | ACT206 |
E | HOH303 |
E | HOH305 |
site_id | DC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA E 203 |
Chain | Residue |
E | HIS17 |
E | ARG90 |
E | SER128 |
E | COA202 |
site_id | DC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS E 204 |
Chain | Residue |
E | LYS15 |
E | GLY18 |
E | ASP19 |
site_id | DC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT E 205 |
Chain | Residue |
E | SER25 |
E | ARG26 |
E | LEU27 |
E | PHE28 |
site_id | DC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT E 206 |
Chain | Residue |
E | TYR6 |
E | ARG87 |
E | GLY88 |
E | ARG90 |
E | COA202 |
site_id | DC5 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE COA F 201 |
Chain | Residue |
C | LEU130 |
C | LEU137 |
F | PRO7 |
F | GLY8 |
F | THR9 |
F | PHE10 |
F | HIS17 |
F | ALA36 |
F | ALA37 |
F | SER38 |
F | LYS41 |
F | PHE69 |
F | SER70 |
F | THR71 |
F | LEU72 |
F | LEU73 |
F | ARG87 |
F | TYR97 |
F | LEU101 |
F | SER127 |
F | SER128 |
F | THR129 |
F | CA203 |
F | ACT206 |
F | HOH305 |
F | HOH310 |
F | HOH318 |
site_id | DC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE POP F 202 |
Chain | Residue |
F | LYS15 |
F | GLY18 |
F | ASP19 |
F | GLU22 |
F | VAL57 |
site_id | DC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA F 203 |
Chain | Residue |
F | HIS17 |
F | SER128 |
F | COA201 |
F | HOH314 |
site_id | DC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS F 204 |
Chain | Residue |
B | ARG26 |
F | ASN83 |
F | ASP111 |
site_id | DC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS F 205 |
Chain | Residue |
F | MET1 |
F | ARG3 |
F | LYS81 |
site_id | EC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT F 206 |
Chain | Residue |
F | TYR6 |
F | ARG87 |
F | GLY88 |
F | ARG90 |
F | COA201 |