3NBK
Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis in complex with 4'-phosphopantetheine
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 |
| A | 0034214 | biological_process | protein hexamerization |
| 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 |
| B | 0034214 | biological_process | protein hexamerization |
| 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 |
| C | 0034214 | biological_process | protein hexamerization |
| 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 |
| D | 0034214 | biological_process | protein hexamerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PNS A 200 |
| Chain | Residue |
| A | GLY8 |
| A | HOH186 |
| A | HOH203 |
| A | HOH204 |
| A | HOH222 |
| A | HOH355 |
| A | HOH357 |
| A | HOH412 |
| A | HOH720 |
| A | HOH1008 |
| A | SER9 |
| A | GLY71 |
| A | LEU72 |
| A | VAL73 |
| A | ASN105 |
| A | GLU132 |
| A | HOH172 |
| A | HOH177 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PNS B 200 |
| Chain | Residue |
| B | GLY8 |
| B | SER9 |
| B | GLY71 |
| B | LEU72 |
| B | VAL73 |
| B | ASN105 |
| B | GLU132 |
| B | LEU136 |
| B | HOH175 |
| B | HOH178 |
| B | HOH191 |
| B | HOH194 |
| B | HOH195 |
| B | HOH203 |
| B | HOH279 |
| B | HOH337 |
| B | HOH347 |
| B | HOH379 |
| B | HOH648 |
| B | HOH687 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PNS C 200 |
| Chain | Residue |
| C | GLY8 |
| C | SER9 |
| C | GLY71 |
| C | LEU72 |
| C | VAL73 |
| C | ASN105 |
| C | GLU132 |
| C | HOH168 |
| C | HOH172 |
| C | HOH182 |
| C | HOH188 |
| C | HOH194 |
| C | HOH205 |
| C | HOH291 |
| C | HOH354 |
| C | HOH452 |
| C | HOH518 |
| C | HOH642 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PNS D 200 |
| Chain | Residue |
| D | GLY8 |
| D | SER9 |
| D | GLY71 |
| D | LEU72 |
| D | VAL73 |
| D | ASN105 |
| D | GLU132 |
| D | HOH171 |
| D | HOH179 |
| D | HOH210 |
| D | HOH322 |
| D | HOH325 |
| D | HOH416 |
| D | HOH436 |
| D | HOH531 |
| D | HOH807 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NI C 162 |
| Chain | Residue |
| C | ARG-3 |
| C | HIS0 |
| C | ASP29 |
| D | ARG-3 |
| D | HIS0 |
| D | ASP29 |
| D | HOH255 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI A 162 |
| Chain | Residue |
| A | HIS0 |
| A | ASP29 |
| B | HIS0 |
| B | ASP29 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:20851704, ECO:0007744|PDB:3NBK |
| Chain | Residue | Details |
| A | SER9 | |
| A | VAL73 | |
| B | SER9 | |
| B | VAL73 | |
| C | SER9 | |
| C | VAL73 | |
| D | SER9 | |
| D | VAL73 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:23151631, ECO:0000305|PubMed:20851704, ECO:0007744|PDB:3NBA, ECO:0007744|PDB:3UC5 |
| Chain | Residue | Details |
| A | HIS17 | |
| D | HIS17 | |
| D | GLY88 | |
| D | TYR122 | |
| A | GLY88 | |
| A | TYR122 | |
| B | HIS17 | |
| B | GLY88 | |
| B | TYR122 | |
| C | HIS17 | |
| C | GLY88 | |
| C | TYR122 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151 |
| Chain | Residue | Details |
| A | LYS41 | |
| A | LYS87 | |
| B | LYS41 | |
| B | LYS87 | |
| C | LYS41 | |
| C | LYS87 | |
| D | LYS41 | |
| D | LYS87 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:23151631, ECO:0007744|PDB:3UC5 |
| Chain | Residue | Details |
| A | GLU98 | |
| B | GLU98 | |
| C | GLU98 | |
| D | GLU98 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20851704, ECO:0007744|PDB:3NBK |
| Chain | Residue | Details |
| A | ASN105 | |
| B | ASN105 | |
| C | ASN105 | |
| D | ASN105 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23151631, ECO:0000305|PubMed:20851704, ECO:0007744|PDB:3NBA, ECO:0007744|PDB:3UC5 |
| Chain | Residue | Details |
| A | THR118 | |
| B | THR118 | |
| C | THR118 | |
| D | THR118 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151 |
| Chain | Residue | Details |
| A | HIS17 | |
| B | HIS17 | |
| C | HIS17 | |
| D | HIS17 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
| Chain | Residue | Details |
| A | THR2 | |
| B | THR2 | |
| C | THR2 | |
| D | THR2 |
