3ND6
Crystal structure of phosphopantetheine adenylyltransferase (PPAT) in complex with ATP from Enterococcus faecalis
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 |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0015937 | biological_process | coenzyme A biosynthetic process |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009058 | biological_process | biosynthetic process |
| E | 0015937 | biological_process | coenzyme A biosynthetic process |
| E | 0016779 | molecular_function | nucleotidyltransferase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009058 | biological_process | biosynthetic process |
| F | 0015937 | biological_process | coenzyme A biosynthetic process |
| F | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP A 961 |
| Chain | Residue |
| A | PHE7 |
| A | TYR125 |
| A | VAL128 |
| A | SER129 |
| A | SER130 |
| A | SER131 |
| A | HOH185 |
| A | HOH192 |
| A | HOH200 |
| A | HOH218 |
| A | HOH260 |
| A | GLY17 |
| A | HOH304 |
| A | HOH319 |
| A | HIS18 |
| A | LEU21 |
| A | ARG89 |
| A | GLY90 |
| A | ARG92 |
| A | GLU100 |
| A | ALA121 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ATP B 962 |
| Chain | Residue |
| B | PHE7 |
| B | GLY9 |
| B | SER10 |
| B | PHE11 |
| B | GLY17 |
| B | HIS18 |
| B | LEU21 |
| B | ARG89 |
| B | GLY90 |
| B | ASP96 |
| B | GLU100 |
| B | ALA121 |
| B | TYR125 |
| B | VAL128 |
| B | SER129 |
| B | SER130 |
| B | SER131 |
| B | HOH187 |
| B | HOH190 |
| B | HOH194 |
| B | HOH202 |
| B | HOH209 |
| B | HOH212 |
| B | HOH264 |
| B | HOH344 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATP C 963 |
| Chain | Residue |
| C | PHE7 |
| C | GLY9 |
| C | SER10 |
| C | GLY17 |
| C | HIS18 |
| C | LEU21 |
| C | ARG89 |
| C | GLY90 |
| C | GLU100 |
| C | ALA121 |
| C | TYR125 |
| C | VAL128 |
| C | SER129 |
| C | SER130 |
| C | SER131 |
| C | HOH183 |
| C | HOH185 |
| C | HOH189 |
| C | HOH190 |
| C | HOH215 |
| C | HOH332 |
| C | HOH366 |
| C | HOH413 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ATP D 964 |
| Chain | Residue |
| D | PHE7 |
| D | GLY9 |
| D | SER10 |
| D | PHE11 |
| D | GLY17 |
| D | HIS18 |
| D | LEU21 |
| D | ARG89 |
| D | GLY90 |
| D | ARG92 |
| D | ASP96 |
| D | GLU100 |
| D | ALA121 |
| D | TYR125 |
| D | VAL128 |
| D | SER129 |
| D | SER130 |
| D | SER131 |
| D | HOH178 |
| D | HOH193 |
| D | HOH196 |
| D | HOH292 |
| D | HOH309 |
| D | HOH320 |
| D | HOH323 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP E 965 |
| Chain | Residue |
| E | LEU21 |
| E | ARG89 |
| E | GLY90 |
| E | GLU100 |
| E | ALA121 |
| E | TYR125 |
| E | VAL128 |
| E | SER129 |
| E | SER130 |
| E | SER131 |
| E | HOH174 |
| E | HOH182 |
| E | HOH206 |
| E | HOH233 |
| E | PHE7 |
| E | GLY9 |
| E | SER10 |
| E | GLY17 |
| E | HIS18 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP F 966 |
| Chain | Residue |
| F | PHE7 |
| F | SER10 |
| F | PHE11 |
| F | GLY17 |
| F | HIS18 |
| F | ARG89 |
| F | GLY90 |
| F | GLU100 |
| F | ALA121 |
| F | TYR125 |
| F | VAL128 |
| F | SER129 |
| F | SER130 |
| F | SER131 |
| F | HOH175 |
| F | HOH190 |
| F | HOH200 |
| F | HOH365 |
| F | HOH392 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
| Chain | Residue | Details |
| A | SER10 | |
| D | SER10 | |
| D | LYS42 | |
| D | ARG89 | |
| E | SER10 | |
| E | LYS42 | |
| E | ARG89 | |
| F | SER10 | |
| F | LYS42 | |
| F | ARG89 | |
| A | LYS42 | |
| A | ARG89 | |
| B | SER10 | |
| B | LYS42 | |
| B | ARG89 | |
| C | SER10 | |
| C | LYS42 | |
| C | ARG89 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6 |
| Chain | Residue | Details |
| A | HIS18 | |
| C | GLY90 | |
| C | GLU100 | |
| C | TYR125 | |
| D | HIS18 | |
| D | GLY90 | |
| D | GLU100 | |
| D | TYR125 | |
| E | HIS18 | |
| E | GLY90 | |
| E | GLU100 | |
| A | GLY90 | |
| E | TYR125 | |
| F | HIS18 | |
| F | GLY90 | |
| F | GLU100 | |
| F | TYR125 | |
| A | GLU100 | |
| A | TYR125 | |
| B | HIS18 | |
| B | GLY90 | |
| B | GLU100 | |
| B | TYR125 | |
| C | HIS18 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21912874, ECO:0007744|PDB:3ND7 |
| Chain | Residue | Details |
| A | THR75 | |
| B | THR75 | |
| C | THR75 | |
| D | THR75 | |
| E | THR75 | |
| F | THR75 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151 |
| Chain | Residue | Details |
| A | HIS18 | |
| B | HIS18 | |
| C | HIS18 | |
| D | HIS18 | |
| E | HIS18 | |
| F | HIS18 |
