5O0B
Crystal structure of Phosphopantetheine adenylyltransferase from Mycobacterium abcessus in complex with 3-Bromo-1H-indazole-5-carboxylic acid (Fragment 2)
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 | 9 |
| Details | binding site for residue 9FE A 201 |
| Chain | Residue |
| A | CYS6 |
| A | GLY8 |
| A | SER9 |
| A | PHE10 |
| A | HIS17 |
| A | GLY88 |
| A | 9FE202 |
| A | HOH352 |
| A | HOH376 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue 9FE A 202 |
| Chain | Residue |
| A | HIS17 |
| A | GLY88 |
| A | ARG90 |
| A | ASP94 |
| A | SER126 |
| A | SER127 |
| A | 9FE201 |
| A | HOH307 |
| A | HOH316 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue 9FE B 201 |
| Chain | Residue |
| B | CYS6 |
| B | SER9 |
| B | PHE10 |
| B | HIS17 |
| B | GLY88 |
| B | 9FE202 |
| B | HOH309 |
| B | HOH347 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue 9FE B 202 |
| Chain | Residue |
| B | GLY16 |
| B | HIS17 |
| B | GLY88 |
| B | ARG90 |
| B | ASP94 |
| B | SER126 |
| B | SER127 |
| B | 9FE201 |
| B | HOH304 |
| B | HOH381 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue 9FE C 201 |
| Chain | Residue |
| C | GLY8 |
| C | SER9 |
| C | PHE10 |
| C | HIS17 |
| C | LYS87 |
| C | GLY88 |
| C | 9FE202 |
| C | HOH329 |
| C | HOH341 |
| C | HOH355 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue 9FE C 202 |
| Chain | Residue |
| C | GLY16 |
| C | HIS17 |
| C | GLY88 |
| C | ARG90 |
| C | ASP94 |
| C | SER126 |
| C | SER127 |
| C | 9FE201 |
| C | HOH301 |
| C | HOH320 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
