5TS2
Crystal structure of a phosphopantetheine adenylyltransferase (CoaD, PPAT) from Pseudomonas aeruginosa bound to dephospho coenzyme A
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 | 20 |
Details | binding site for residue COD A 201 |
Chain | Residue |
A | TYR6 |
A | LEU73 |
A | ARG87 |
A | GLY88 |
A | ARG90 |
A | LEU101 |
A | ASN105 |
A | PRO119 |
A | TYR123 |
A | ILE126 |
A | HOH315 |
A | PRO7 |
E | LEU137 |
A | GLY8 |
A | THR9 |
A | PHE10 |
A | GLY16 |
A | HIS17 |
A | THR71 |
A | LEU72 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 202 |
Chain | Residue |
A | HIS-3 |
A | HIS-5 |
C | HIS-3 |
C | HIS-5 |
E | HIS-3 |
E | HIS-5 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CL A 203 |
Chain | Residue |
A | SER127 |
A | THR129 |
site_id | AC4 |
Number of Residues | 22 |
Details | binding site for residue COD B 201 |
Chain | Residue |
B | TYR6 |
B | PRO7 |
B | GLY8 |
B | THR9 |
B | PHE10 |
B | GLY16 |
B | HIS17 |
B | PHE69 |
B | LEU72 |
B | LEU73 |
B | ARG87 |
B | GLY88 |
B | ARG90 |
B | TYR97 |
B | GLU98 |
B | ASN105 |
B | PRO119 |
B | TYR123 |
B | ILE126 |
B | HOH301 |
B | HOH303 |
B | HOH306 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue CL B 202 |
Chain | Residue |
B | SER127 |
B | THR129 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue CL B 203 |
Chain | Residue |
B | ALA109 |
B | PRO110 |
B | ASP111 |
site_id | AC7 |
Number of Residues | 19 |
Details | binding site for residue COD C 201 |
Chain | Residue |
A | LEU137 |
C | TYR6 |
C | PRO7 |
C | GLY8 |
C | THR9 |
C | PHE10 |
C | GLY16 |
C | HIS17 |
C | LYS41 |
C | LEU72 |
C | LEU73 |
C | ARG87 |
C | GLY88 |
C | ARG90 |
C | TYR97 |
C | PRO119 |
C | TYR123 |
C | ILE126 |
C | HOH325 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue CL C 202 |
Chain | Residue |
C | SER127 |
C | THR129 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue CL C 203 |
Chain | Residue |
C | ALA109 |
C | PRO110 |
C | ASP111 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue CL C 204 |
Chain | Residue |
C | HIS-5 |
C | HIS-4 |
C | HIS0 |
site_id | AD2 |
Number of Residues | 22 |
Details | binding site for residue COD D 201 |
Chain | Residue |
D | ILE126 |
D | HOH326 |
D | HOH330 |
F | LEU130 |
F | GLU133 |
D | TYR6 |
D | PRO7 |
D | GLY8 |
D | THR9 |
D | PHE10 |
D | GLY16 |
D | HIS17 |
D | THR71 |
D | LEU72 |
D | LEU73 |
D | ARG87 |
D | GLY88 |
D | ARG90 |
D | LEU101 |
D | ASN105 |
D | PRO119 |
D | TYR123 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue CL D 202 |
Chain | Residue |
D | SER127 |
D | THR129 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue CL D 203 |
Chain | Residue |
D | ALA109 |
D | PRO110 |
D | ASP111 |
site_id | AD5 |
Number of Residues | 21 |
Details | binding site for residue COD E 201 |
Chain | Residue |
C | LEU130 |
C | LEU137 |
E | TYR6 |
E | PRO7 |
E | GLY8 |
E | THR9 |
E | PHE10 |
E | GLY16 |
E | HIS17 |
E | PHE69 |
E | LEU72 |
E | LEU73 |
E | ARG87 |
E | GLY88 |
E | ARG90 |
E | GLU98 |
E | LEU101 |
E | PRO119 |
E | TYR123 |
E | ILE126 |
E | HOH323 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue CA E 202 |
Chain | Residue |
C | HOH322 |
E | VAL64 |
E | HOH311 |
E | HOH319 |
E | HOH330 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue CL E 203 |
Chain | Residue |
E | ALA109 |
E | PRO110 |
E | ASP111 |
site_id | AD8 |
Number of Residues | 25 |
Details | binding site for residue COD F 201 |
Chain | Residue |
B | GLU133 |
B | LEU137 |
F | TYR6 |
F | PRO7 |
F | GLY8 |
F | THR9 |
F | PHE10 |
F | GLY16 |
F | HIS17 |
F | LYS41 |
F | LEU72 |
F | LEU73 |
F | ARG87 |
F | GLY88 |
F | ARG90 |
F | GLU98 |
F | LEU101 |
F | ASN105 |
F | PRO119 |
F | TYR123 |
F | ILE126 |
F | HOH304 |
F | HOH310 |
F | HOH311 |
F | HOH316 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue CL F 202 |
Chain | Residue |
F | SER127 |
F | THR129 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue CL F 203 |
Chain | Residue |
F | ALA109 |
F | PRO110 |
F | ASP111 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 48 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | THR9 | |
B | HIS17 | |
B | LYS41 | |
B | LEU73 | |
B | ARG87 | |
B | GLY88 | |
B | GLU98 | |
B | TYR123 | |
C | THR9 | |
C | HIS17 | |
C | LYS41 | |
A | HIS17 | |
C | LEU73 | |
C | ARG87 | |
C | GLY88 | |
C | GLU98 | |
C | TYR123 | |
D | THR9 | |
D | HIS17 | |
D | LYS41 | |
D | LEU73 | |
D | ARG87 | |
A | LYS41 | |
D | GLY88 | |
D | GLU98 | |
D | TYR123 | |
E | THR9 | |
E | HIS17 | |
E | LYS41 | |
E | LEU73 | |
E | ARG87 | |
E | GLY88 | |
E | GLU98 | |
A | LEU73 | |
E | TYR123 | |
F | THR9 | |
F | HIS17 | |
F | LYS41 | |
F | LEU73 | |
F | ARG87 | |
F | GLY88 | |
F | GLU98 | |
F | TYR123 | |
A | ARG87 | |
A | GLY88 | |
A | GLU98 | |
A | TYR123 | |
B | THR9 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | HIS17 | |
B | HIS17 | |
C | HIS17 | |
D | HIS17 | |
E | HIS17 | |
F | HIS17 |