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 | 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 | 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 | 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 | 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 | 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 | 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 |