4NAH
Inhibitors of 4-Phosphopanthetheine Adenylyltransferase (PPAT)
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 | 19 |
| Details | BINDING SITE FOR RESIDUE AGS A 201 |
| Chain | Residue |
| A | SER11 |
| A | GLU100 |
| A | SER121 |
| A | TYR125 |
| A | ILE128 |
| A | SER129 |
| A | SER130 |
| A | SER131 |
| A | 2VJ203 |
| A | HOH302 |
| A | HOH313 |
| A | PHE12 |
| A | GLY18 |
| A | HIS19 |
| A | ILE22 |
| A | ARG89 |
| A | GLY90 |
| A | ARG92 |
| A | ASP96 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 2VJ A 202 |
| Chain | Residue |
| A | GLU135 |
| A | VAL136 |
| A | TYR139 |
| A | HOH301 |
| C | CYS36 |
| C | LYS43 |
| C | GLY73 |
| C | LEU74 |
| C | LEU75 |
| C | ARG89 |
| C | TYR99 |
| C | ASN107 |
| C | HOH301 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 2VJ A 203 |
| Chain | Residue |
| A | PRO9 |
| A | SER11 |
| A | CYS36 |
| A | VAL37 |
| A | LEU38 |
| A | GLY73 |
| A | LEU75 |
| A | ARG89 |
| A | TYR99 |
| A | MET106 |
| A | ASN107 |
| A | AGS201 |
| A | HOH304 |
| A | HOH306 |
| B | GLU135 |
| B | TYR139 |
| B | HOH307 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AGS B 201 |
| Chain | Residue |
| B | SER11 |
| B | PHE12 |
| B | GLY18 |
| B | HIS19 |
| B | ARG89 |
| B | GLY90 |
| B | ARG92 |
| B | GLU100 |
| B | SER121 |
| B | TYR125 |
| B | ILE128 |
| B | SER129 |
| B | SER130 |
| B | SER131 |
| B | HOH312 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 2VJ B 202 |
| Chain | Residue |
| B | PRO9 |
| B | CYS36 |
| B | VAL37 |
| B | LEU38 |
| B | GLY73 |
| B | LEU74 |
| B | LEU75 |
| B | ARG89 |
| B | TYR99 |
| B | MET106 |
| B | ASN107 |
| B | HOH301 |
| C | GLU135 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AGS C 201 |
| Chain | Residue |
| C | PRO9 |
| C | SER11 |
| C | PHE12 |
| C | GLY18 |
| C | HIS19 |
| C | ILE22 |
| C | ARG89 |
| C | GLY90 |
| C | ARG92 |
| C | GLU100 |
| C | SER121 |
| C | TYR125 |
| C | ILE128 |
| C | SER129 |
| C | SER130 |
| C | SER131 |
| C | HOH302 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AGS D 201 |
| Chain | Residue |
| D | ILE22 |
| D | ARG89 |
| D | GLY90 |
| D | ARG92 |
| D | GLU100 |
| D | SER121 |
| D | TYR125 |
| D | ILE128 |
| D | SER129 |
| D | SER130 |
| D | SER131 |
| D | HOH303 |
| D | HOH305 |
| D | PRO9 |
| D | SER11 |
| D | PHE12 |
| D | GLY18 |
| D | HIS19 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2VJ D 202 |
| Chain | Residue |
| D | PRO9 |
| D | GLY10 |
| D | CYS36 |
| D | VAL37 |
| D | GLY73 |
| D | LEU75 |
| D | ARG89 |
| D | TYR99 |
| D | MET106 |
| D | ASN107 |
| D | HOH301 |
| E | GLU135 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AGS E 201 |
| Chain | Residue |
| E | SER11 |
| E | PHE12 |
| E | GLY18 |
| E | HIS19 |
| E | ARG89 |
| E | GLY90 |
| E | ARG92 |
| E | ASP96 |
| E | GLU100 |
| E | SER121 |
| E | TYR125 |
| E | ILE128 |
| E | SER129 |
| E | SER130 |
| E | SER131 |
| E | HOH303 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AGS F 201 |
| Chain | Residue |
| F | GLY10 |
| F | SER11 |
| F | PHE12 |
| F | GLY18 |
| F | HIS19 |
| F | ILE22 |
| F | ARG89 |
| F | GLY90 |
| F | ARG92 |
| F | SER121 |
| F | TYR125 |
| F | ILE128 |
| F | SER129 |
| F | SER130 |
| F | SER131 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 2VJ F 202 |
| Chain | Residue |
| E | PRO9 |
| E | CYS36 |
| E | GLY73 |
| E | LEU75 |
| E | TYR99 |
| E | LEU103 |
| E | ASN107 |
| F | GLU135 |
| F | VAL136 |
| F | TYR139 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2VJ F 203 |
| Chain | Residue |
| D | GLU135 |
| D | TYR139 |
| F | PRO9 |
| F | CYS36 |
| F | GLY73 |
| F | LEU74 |
| F | LEU75 |
| F | ARG89 |
| F | TYR99 |
| F | GLU100 |
| F | ASN107 |
| F | HOH302 |
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 | SER11 | |
| C | LYS43 | |
| C | LEU75 | |
| C | ARG89 | |
| D | SER11 | |
| D | LYS43 | |
| D | LEU75 | |
| D | ARG89 | |
| E | SER11 | |
| E | LYS43 | |
| E | LEU75 | |
| A | LYS43 | |
| E | ARG89 | |
| F | SER11 | |
| F | LYS43 | |
| F | LEU75 | |
| F | ARG89 | |
| A | LEU75 | |
| A | ARG89 | |
| B | SER11 | |
| B | LYS43 | |
| B | LEU75 | |
| B | ARG89 | |
| C | SER11 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAU |
| Chain | Residue | Details |
| A | HIS19 | |
| E | TYR125 | |
| F | HIS19 | |
| F | TYR125 | |
| A | TYR125 | |
| B | HIS19 | |
| B | TYR125 | |
| C | HIS19 | |
| C | TYR125 | |
| D | HIS19 | |
| D | TYR125 | |
| E | HIS19 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| 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 | |
| D | GLY90 | |
| E | GLY90 | |
| F | GLY90 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| 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 | |
| D | GLU100 | |
| E | GLU100 | |
| F | GLU100 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH, ECO:0007744|PDB:4NAU |
| Chain | Residue | Details |
| A | SER121 | |
| B | SER121 | |
| C | SER121 | |
| D | SER121 | |
| E | SER121 | |
| F | SER121 |
