3L92
Phosphopantetheine adenylyltransferase from Yersinia pestis complexed with coenzyme A.
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE COA A 301 |
| Chain | Residue |
| A | GLY9 |
| A | ARG91 |
| A | ASP95 |
| A | TYR98 |
| A | GLU99 |
| A | LEU102 |
| A | MET105 |
| A | ASN106 |
| A | SER128 |
| A | SER129 |
| A | SER130 |
| A | THR10 |
| A | GLU134 |
| A | HIS138 |
| A | HOH165 |
| A | HOH168 |
| A | HOH172 |
| A | HOH173 |
| A | HOH184 |
| A | HOH201 |
| A | HOH212 |
| A | HOH218 |
| A | PHE11 |
| A | HOH225 |
| A | HOH230 |
| A | HOH244 |
| A | HOH256 |
| A | HOH286 |
| A | HOH291 |
| A | HOH294 |
| A | HOH295 |
| A | HOH297 |
| A | HOH298 |
| A | HIS18 |
| A | ALA37 |
| A | LYS42 |
| A | LEU73 |
| A | MET74 |
| A | ARG88 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"PDB data bank","title":"X-ray crystal structure of phosphopantetheine adenylyltransferase from Yersinia pestis.","authors":["Osipiuk J.","Maltseva N.","Makowska-grzyska M.","Kwon K.","Anderson W.F.","Joachimiak A."]}},{"source":"PDB","id":"3L92","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"PDB data bank","title":"X-ray crystal structure of phosphopantetheine adenylyltransferase from Yersinia pestis.","authors":["Osipiuk J.","Maltseva N.","Makowska-grzyska M.","Kwon K.","Anderson W.F.","Joachimiak A."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
