4NAT
Inhibitors of 4-Phosphopanthetheine Adenylyltransferase
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 | 12 |
| Details | BINDING SITE FOR RESIDUE 2W5 A 201 |
| Chain | Residue |
| A | PRO9 |
| A | HOH329 |
| B | GLU135 |
| B | TYR139 |
| A | CYS36 |
| A | PHE71 |
| A | GLY73 |
| A | LEU74 |
| A | LEU75 |
| A | LEU103 |
| A | ASN107 |
| A | HOH317 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EPE A 202 |
| Chain | Residue |
| A | LEU74 |
| A | ASP77 |
| A | LEU110 |
| B | TYR139 |
| B | ARG140 |
| B | ALA141 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ADP A 203 |
| Chain | Residue |
| A | PRO9 |
| A | GLY10 |
| A | SER11 |
| A | PHE12 |
| A | HIS19 |
| A | ARG89 |
| A | HOH335 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 2W5 B 201 |
| Chain | Residue |
| B | PRO9 |
| B | CYS36 |
| B | PHE71 |
| B | GLY73 |
| B | LEU74 |
| B | LEU75 |
| B | ARG89 |
| B | LEU103 |
| B | MET106 |
| B | ASN107 |
| B | HOH323 |
| B | HOH337 |
| C | GLU135 |
| C | TYR139 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EPE B 202 |
| Chain | Residue |
| A | TYR139 |
| A | ARG140 |
| A | ALA141 |
| C | LEU74 |
| C | ASP77 |
| C | LEU110 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ADP B 203 |
| Chain | Residue |
| B | GLY10 |
| B | SER11 |
| B | PHE12 |
| B | HIS19 |
| B | ARG89 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 2W5 C 201 |
| Chain | Residue |
| A | GLU135 |
| A | VAL136 |
| C | PRO9 |
| C | CYS36 |
| C | LEU38 |
| C | GLY73 |
| C | LEU74 |
| C | LEU75 |
| C | ARG89 |
| C | MET106 |
| C | ASN107 |
| C | ADP202 |
| C | HOH319 |
| C | HOH338 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP C 202 |
| Chain | Residue |
| C | GLY10 |
| C | SER11 |
| C | PHE12 |
| C | HIS19 |
| C | ARG89 |
| C | ARG92 |
| C | TYR99 |
| C | 2W5201 |
| C | HOH340 |
| C | HOH342 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
| Chain | Residue | Details |
| A | SER11 | |
| C | LYS43 | |
| C | LEU75 | |
| C | ARG89 | |
| A | LYS43 | |
| A | LEU75 | |
| A | ARG89 | |
| B | SER11 | |
| B | LYS43 | |
| B | LEU75 | |
| B | ARG89 | |
| C | SER11 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAU |
| Chain | Residue | Details |
| A | HIS19 | |
| A | TYR125 | |
| B | HIS19 | |
| B | TYR125 | |
| C | HIS19 | |
| C | TYR125 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| 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 | |
| B | GLY90 | |
| C | GLY90 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH |
| Chain | Residue | Details |
| A | GLU100 | |
| B | GLU100 | |
| C | GLU100 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH, ECO:0007744|PDB:4NAU |
| Chain | Residue | Details |
| A | SER121 | |
| B | SER121 | |
| C | SER121 |
