3K9W
Crystal structure of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei with hydrolyzed 3'-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 | 0009058 | biological_process | biosynthetic process |
A | 0015937 | biological_process | coenzyme A biosynthetic process |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE 4PS A 167 |
Chain | Residue |
A | GLY8 |
A | ARG87 |
A | TYR97 |
A | ASN105 |
A | ILE130 |
A | GLU133 |
A | LEU137 |
A | HOH184 |
A | HOH214 |
A | HOH232 |
A | HOH262 |
A | THR9 |
A | HOH266 |
A | HOH301 |
A | HOH306 |
A | PHE10 |
A | HIS17 |
A | ALA36 |
A | LYS41 |
A | GLY71 |
A | LEU72 |
A | LEU73 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ADE A 168 |
Chain | Residue |
A | GLY16 |
A | ARG90 |
A | PRO119 |
A | TYR123 |
A | ILE126 |
A | ACT170 |
A | SO4171 |
A | HOH197 |
A | HOH306 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PG4 A 169 |
Chain | Residue |
A | ASP37 |
A | PHE45 |
A | SER46 |
A | LEU47 |
A | GLU48 |
A | ARG50 |
A | GLU155 |
A | ALA158 |
A | ALA159 |
A | HOH225 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 170 |
Chain | Residue |
A | SER127 |
A | GLY128 |
A | THR129 |
A | ADE168 |
A | HOH193 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 171 |
Chain | Residue |
A | ARG90 |
A | SER93 |
A | ASP94 |
A | TYR97 |
A | GLU98 |
A | ADE168 |
A | HOH307 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3PXU |
Chain | Residue | Details |
A | TYR6 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | THR9 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3PXU |
Chain | Residue | Details |
A | HIS17 | |
A | GLY88 | |
A | GLU98 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21904046, ECO:0007744|PDB:3K9W, ECO:0007744|PDB:3PXU |
Chain | Residue | Details |
A | LYS41 | |
A | LEU73 | |
A | ARG87 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21904046 |
Chain | Residue | Details |
A | TYR123 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | HIS17 |