5KYV
Structure of Photinus pyralis Luciferase green shifted light emitting variant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001676 | biological_process | long-chain fatty acid metabolic process |
| A | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005777 | cellular_component | peroxisome |
| A | 0008218 | biological_process | bioluminescence |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
| A | 0047077 | molecular_function | Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0001676 | biological_process | long-chain fatty acid metabolic process |
| B | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005777 | cellular_component | peroxisome |
| B | 0008218 | biological_process | bioluminescence |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
| B | 0047077 | molecular_function | Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue SLU A 601 |
| Chain | Residue |
| A | HIS245 |
| A | GLY341 |
| A | LEU342 |
| A | THR343 |
| A | SER347 |
| A | ALA348 |
| A | VAL362 |
| A | ASP422 |
| A | ARG437 |
| A | LEU526 |
| A | ALA246 |
| A | PHE247 |
| A | GLY315 |
| A | GLY316 |
| A | ALA317 |
| A | PRO318 |
| A | GLN338 |
| A | GLY339 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue TLA A 602 |
| Chain | Residue |
| A | PRO225 |
| A | ASN229 |
| A | GLN230 |
| A | HIS310 |
| A | GLU354 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue SLU B 601 |
| Chain | Residue |
| B | HIS245 |
| B | PHE247 |
| B | THR251 |
| B | GLY315 |
| B | GLY316 |
| B | ALA317 |
| B | PRO318 |
| B | GLN338 |
| B | GLY339 |
| B | TYR340 |
| B | GLY341 |
| B | LEU342 |
| B | THR343 |
| B | SER347 |
| B | ALA348 |
| B | ASP422 |
| B | ARG437 |
| B | LYS529 |
| B | HOH707 |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. IMNSSGSTGlPK |
| Chain | Residue | Details |
| A | ILE195-LYS206 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 128 |
| Chain | Residue | Details |
| A | ARG218 | electrostatic stabiliser |
| A | HIS245 | electrostatic stabiliser |
| A | THR343 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS443 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS529 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 128 |
| Chain | Residue | Details |
| B | ARG218 | electrostatic stabiliser |
| B | HIS245 | electrostatic stabiliser |
| B | THR343 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS443 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS529 | electrostatic stabiliser, hydrogen bond donor |
