3F3M
Six Crystal Structures of Two Phosphopantetheine Adenylyltransferases Reveal an Alternative Ligand Binding Mode and an Associated Structural Change
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 | 15 |
Details | BINDING SITE FOR RESIDUE PPS A 300 |
Chain | Residue |
A | GLY10 |
A | SER129 |
A | SER130 |
A | SER131 |
A | HOH169 |
A | HOH170 |
A | HOH191 |
A | SER11 |
A | GLY18 |
A | HIS19 |
A | ILE22 |
A | ARG89 |
A | ARG92 |
A | TYR99 |
A | ILE128 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
Chain | Residue | Details |
A | SER11 | |
A | LYS43 | |
A | LEU75 | |
A | ARG89 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAU |
Chain | Residue | Details |
A | HIS19 | |
A | TYR125 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAT, ECO:0007744|PDB:4NAU |
Chain | Residue | Details |
A | GLY90 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH |
Chain | Residue | Details |
A | GLU100 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH, ECO:0007744|PDB:4NAU |
Chain | Residue | Details |
A | SER121 |