5O08
Crystal structure of Phosphopantetheine adenylyltransferase from Mycobacterium abcessus in complex with Dephospho-coenzyme A
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 | 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| 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 | 0009058 | biological_process | biosynthetic process |
| C | 0015937 | biological_process | coenzyme A biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | binding site for residue COD A 201 |
| Chain | Residue |
| A | GLY8 |
| A | LEU73 |
| A | LYS87 |
| A | GLY88 |
| A | ARG90 |
| A | TYR97 |
| A | GLU98 |
| A | ASN105 |
| A | THR118 |
| A | TYR122 |
| A | VAL125 |
| A | SER9 |
| A | HOH322 |
| A | HOH331 |
| A | HOH339 |
| A | HOH341 |
| A | HOH346 |
| A | HOH350 |
| A | HOH360 |
| A | HOH361 |
| A | HOH366 |
| C | GLU132 |
| A | PHE10 |
| C | EDO202 |
| A | GLY16 |
| A | HIS17 |
| A | VAL20 |
| A | ASN38 |
| A | LYS41 |
| A | LEU72 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 202 |
| Chain | Residue |
| A | SER9 |
| A | LEU36 |
| A | ILE37 |
| A | ASN38 |
| A | LYS41 |
| A | GLY43 |
| A | ARG50 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 203 |
| Chain | Residue |
| A | ALA121 |
| A | PHE124 |
| A | HOH368 |
| B | HIS107 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue COD B 201 |
| Chain | Residue |
| A | GLU132 |
| A | HOH313 |
| B | GLY8 |
| B | SER9 |
| B | PHE10 |
| B | GLY16 |
| B | HIS17 |
| B | VAL20 |
| B | ASN38 |
| B | GLY71 |
| B | LEU72 |
| B | LEU73 |
| B | LYS87 |
| B | GLY88 |
| B | ARG90 |
| B | TYR97 |
| B | GLU98 |
| B | ASN105 |
| B | THR118 |
| B | TYR122 |
| B | HOH323 |
| B | HOH328 |
| B | HOH348 |
| B | HOH350 |
| B | HOH351 |
| B | HOH358 |
| B | HOH359 |
| B | HOH360 |
| B | HOH364 |
| B | HOH373 |
| B | HOH379 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 202 |
| Chain | Residue |
| B | GLU132 |
| C | ASN38 |
| C | ASN40 |
| C | TYR97 |
| C | COD201 |
| site_id | AC6 |
| Number of Residues | 32 |
| Details | binding site for residue COD C 201 |
| Chain | Residue |
| C | HOH324 |
| C | HOH326 |
| C | HOH327 |
| C | HOH341 |
| C | HOH345 |
| C | HOH352 |
| C | HOH357 |
| C | HOH358 |
| C | HOH359 |
| C | HOH372 |
| B | GLU132 |
| B | EDO202 |
| C | GLY8 |
| C | SER9 |
| C | PHE10 |
| C | GLY16 |
| C | HIS17 |
| C | VAL20 |
| C | ASN38 |
| C | LYS41 |
| C | GLY71 |
| C | LEU72 |
| C | LEU73 |
| C | LYS87 |
| C | GLY88 |
| C | ARG90 |
| C | TYR97 |
| C | GLU98 |
| C | ASN105 |
| C | THR118 |
| C | TYR122 |
| C | VAL125 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 202 |
| Chain | Residue |
| A | ASN38 |
| A | PRO39 |
| A | ASN40 |
| A | TYR97 |
| A | COD201 |
| A | HOH359 |
| C | GLU132 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
| Chain | Residue | Details |
| A | SER9 | |
| B | HIS17 | |
| B | LYS41 | |
| B | LEU73 | |
| B | LYS87 | |
| B | GLY88 | |
| B | GLU98 | |
| B | TYR122 | |
| C | SER9 | |
| C | HIS17 | |
| C | LYS41 | |
| A | HIS17 | |
| C | LEU73 | |
| C | LYS87 | |
| C | GLY88 | |
| C | GLU98 | |
| C | TYR122 | |
| A | LYS41 | |
| A | LEU73 | |
| A | LYS87 | |
| A | GLY88 | |
| A | GLU98 | |
| A | TYR122 | |
| B | SER9 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151 |
| Chain | Residue | Details |
| A | HIS17 | |
| B | HIS17 | |
| C | HIS17 |
