1VLH
Crystal structure of Phosphopantetheine adenylyltransferase (TM0741) from Thermotoga maritima at 2.20 A resolution
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 |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| E | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| E | 0016779 | molecular_function | nucleotidyltransferase activity |
| F | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| F | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PNS A 200 |
| Chain | Residue |
| A | GLY7 |
| A | ARG86 |
| A | TYR96 |
| A | ASN104 |
| A | HOH207 |
| A | HOH212 |
| A | HOH221 |
| E | GLU132 |
| A | SER8 |
| A | THR35 |
| A | GLU36 |
| A | ASN37 |
| A | LYS40 |
| A | GLY70 |
| A | LEU71 |
| A | LEU72 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PNS B 200 |
| Chain | Residue |
| B | GLY7 |
| B | SER8 |
| B | THR35 |
| B | GLU36 |
| B | ASN37 |
| B | LYS40 |
| B | GLY70 |
| B | LEU72 |
| B | ARG86 |
| B | TYR96 |
| B | MET100 |
| B | ASN104 |
| B | HOH221 |
| B | HOH236 |
| B | HOH241 |
| F | GLU132 |
| F | TYR136 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PNS C 200 |
| Chain | Residue |
| A | GLU132 |
| A | VAL133 |
| A | TYR136 |
| C | GLY7 |
| C | SER8 |
| C | THR35 |
| C | GLU36 |
| C | ASN37 |
| C | LYS40 |
| C | GLY70 |
| C | LEU71 |
| C | LEU72 |
| C | ARG86 |
| C | MET100 |
| C | ASN104 |
| C | HOH202 |
| C | HOH203 |
| C | HOH236 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PNS D 200 |
| Chain | Residue |
| B | GLU132 |
| B | VAL133 |
| B | TYR136 |
| B | HOH219 |
| D | GLY7 |
| D | SER8 |
| D | THR35 |
| D | GLU36 |
| D | ASN37 |
| D | LYS40 |
| D | GLY70 |
| D | LEU71 |
| D | LEU72 |
| D | ARG86 |
| D | TYR96 |
| D | MET100 |
| D | ASN104 |
| D | HOH202 |
| D | HOH208 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PNS E 200 |
| Chain | Residue |
| C | GLU132 |
| C | TYR136 |
| C | HOH237 |
| E | GLY7 |
| E | SER8 |
| E | THR35 |
| E | GLU36 |
| E | ASN37 |
| E | LYS40 |
| E | LEU71 |
| E | LEU72 |
| E | ARG86 |
| E | TYR96 |
| E | MET100 |
| E | ASN104 |
| E | HOH207 |
| E | HOH212 |
| E | HOH233 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PNS F 200 |
| Chain | Residue |
| F | LEU72 |
| F | ARG86 |
| F | MET100 |
| F | ASN104 |
| F | HOH214 |
| F | HOH227 |
| F | HOH237 |
| D | GLU132 |
| D | TYR136 |
| D | HOH242 |
| F | GLY7 |
| F | SER8 |
| F | THR35 |
| F | GLU36 |
| F | ASN37 |
| F | LYS40 |
| F | GLY70 |
| F | LEU71 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 201 |
| Chain | Residue |
| B | PRO146 |
| B | ARG150 |
| F | ASP28 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 66 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of phosphopantetheine adenylyltransferase (TM0741) from Thermotoga maritima at 2.20 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}},{"source":"PDB","id":"1VLH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of phosphopantetheine adenylyltransferase (TM0741) from Thermotoga maritima at 2.20 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}},{"source":"PDB","id":"1VLH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of phosphopantetheine adenylyltransferase (TM0741) from Thermotoga maritima at 2.20 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}},{"source":"PDB","id":"1VLH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
