3UC5
Phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis complexed with ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0034214 | biological_process | protein hexamerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATP A 1440 |
| Chain | Residue |
| A | PRO7 |
| A | ARG90 |
| A | GLU98 |
| A | THR118 |
| A | TYR122 |
| A | SER126 |
| A | SER127 |
| A | SER128 |
| A | HOH170 |
| A | HOH178 |
| A | HOH181 |
| A | GLY8 |
| A | HOH182 |
| A | HOH191 |
| A | HOH209 |
| A | HOH210 |
| A | SER9 |
| A | PHE10 |
| A | GLY16 |
| A | HIS17 |
| A | ILE20 |
| A | LYS87 |
| A | GLY88 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23151631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20851704","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3NBA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UC5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20851704","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NBK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23151631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UC5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20851704","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NBK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23151631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20851704","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3NBA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UC5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"21969609","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
