6Q2M
Crystal structure of Photinus pyralis Luciferase Pps6 mutant in complex with DLSA
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 |
| C | 0001676 | biological_process | long-chain fatty acid metabolic process |
| C | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005777 | cellular_component | peroxisome |
| C | 0008218 | biological_process | bioluminescence |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
| C | 0047077 | molecular_function | Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity |
| C | 0051087 | molecular_function | protein-folding chaperone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 601 |
| Chain | Residue |
| A | VAL516 |
| A | VAL517 |
| A | PHE518 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue DYD A 602 |
| Chain | Residue |
| A | ASP19 |
| A | GLY20 |
| A | ASP187 |
| A | ARG188 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue DYD A 603 |
| Chain | Residue |
| A | ASP279 |
| A | TYR280 |
| A | ASN50 |
| A | ARG261 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 604 |
| Chain | Residue |
| A | LYS130 |
| C | PRO174 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 605 |
| Chain | Residue |
| A | ASP157 |
| A | GLN159 |
| A | GLY160 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 606 |
| Chain | Residue |
| A | ASN229 |
| A | GLN230 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 607 |
| Chain | Residue |
| A | GLY324 |
| A | GLU325 |
| A | ILE336 |
| A | PRO359 |
| A | HOH714 |
| A | HOH771 |
| A | HOH781 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 608 |
| Chain | Residue |
| A | ASP302 |
| A | TYR304 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 609 |
| Chain | Residue |
| A | ASN385 |
| A | GLN386 |
| A | ARG387 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 610 |
| Chain | Residue |
| A | ARG69 |
| A | HIS171 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 611 |
| Chain | Residue |
| A | ASN84 |
| A | VAL240 |
| A | PRO242 |
| A | MET265 |
| A | HOH801 |
| A | HOH878 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 612 |
| Chain | Residue |
| A | GLU111 |
| A | HOH866 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 613 |
| Chain | Residue |
| A | ASN177 |
| A | ASP180 |
| C | ILE47 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 614 |
| Chain | Residue |
| A | GLY394 |
| A | ILE397 |
| A | HOH823 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 615 |
| Chain | Residue |
| A | PHE368 |
| A | GLU370 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 616 |
| Chain | Residue |
| A | LEU459 |
| A | GLN460 |
| A | HIS461 |
| A | PRO462 |
| A | ILE464 |
| A | GLU488 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 617 |
| Chain | Residue |
| A | TYR70 |
| A | HIS76 |
| A | GLN147 |
| A | HOH761 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 618 |
| Chain | Residue |
| A | LEU342 |
| A | ARG437 |
| A | HOH745 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 619 |
| Chain | Residue |
| A | GLN87 |
| A | ASP153 |
| A | LYS155 |
| site_id | AE2 |
| Number of Residues | 22 |
| Details | binding site for residue SLU A 620 |
| Chain | Residue |
| A | SER199 |
| A | HIS245 |
| A | PHE247 |
| A | THR251 |
| A | GLY316 |
| A | ALA317 |
| A | PRO318 |
| A | GLN338 |
| A | GLY339 |
| A | TYR340 |
| A | GLY341 |
| A | LEU342 |
| A | THR343 |
| A | SER347 |
| A | ALA348 |
| A | VAL362 |
| A | ASP422 |
| A | ARG437 |
| A | LYS529 |
| A | HOH706 |
| A | HOH743 |
| A | HOH813 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 601 |
| Chain | Residue |
| B | GLU370 |
| B | ARG393 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 602 |
| Chain | Residue |
| B | ASP19 |
| B | GLY20 |
| B | ARG188 |
| site_id | AE5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 603 |
| Chain | Residue |
| B | TYR179 |
| B | EDO608 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 604 |
| Chain | Residue |
| A | ASP302 |
| A | ARG330 |
| B | PRO13 |
| B | PHE14 |
| site_id | AE7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 605 |
| Chain | Residue |
| B | GLU55 |
| B | LYS155 |
| site_id | AE8 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 606 |
| Chain | Residue |
| B | SER185 |
| site_id | AE9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 607 |
| Chain | Residue |
| B | ARG218 |
| B | PHE227 |
| B | ILE351 |
| B | SLU611 |
| site_id | AF1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 608 |
| Chain | Residue |
| B | TYR179 |
| B | SO4603 |
| site_id | AF2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 609 |
| Chain | Residue |
| B | SER399 |
| site_id | AF3 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 610 |
| Chain | Residue |
| B | ASN403 |
| site_id | AF4 |
| Number of Residues | 17 |
| Details | binding site for residue SLU B 611 |
| Chain | Residue |
| B | HIS245 |
| B | PHE247 |
| B | THR251 |
| B | SER314 |
| B | GLY316 |
| B | ALA317 |
| B | PRO318 |
| B | GLY339 |
| B | TYR340 |
| B | GLY341 |
| B | LEU342 |
| B | THR343 |
| B | SER347 |
| B | ALA348 |
| B | ASP422 |
| B | ARG437 |
| B | EDO607 |
| site_id | AF5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 601 |
| Chain | Residue |
| C | ASN50 |
| C | ARG261 |
| C | EDO615 |
| site_id | AF6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 602 |
| Chain | Residue |
| C | LYS372 |
| C | ARG393 |
| C | ASP415 |
| C | TRP417 |
| site_id | AF7 |
| Number of Residues | 2 |
| Details | binding site for residue DYD C 603 |
| Chain | Residue |
| A | ASN177 |
| C | GLU83 |
| site_id | AF8 |
| Number of Residues | 1 |
| Details | binding site for residue DYD C 604 |
| Chain | Residue |
| C | VAL288 |
| site_id | AF9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 605 |
| Chain | Residue |
| C | ASP19 |
| C | GLY20 |
| site_id | AG1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 606 |
| Chain | Residue |
| A | GLU55 |
| A | GLU58 |
| C | HIS46 |
| site_id | AG2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 607 |
| Chain | Residue |
| C | ASN75 |
| site_id | AG3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 608 |
| Chain | Residue |
| C | SER170 |
| C | HIS171 |
| C | LEU172 |
| site_id | AG4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 609 |
| Chain | Residue |
| C | ASN177 |
| C | TYR179 |
| site_id | AG5 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 610 |
| Chain | Residue |
| C | ARG77 |
| site_id | AG6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 611 |
| Chain | Residue |
| A | LYS31 |
| A | LEU35 |
| A | TYR179 |
| C | LYS130 |
| C | TYR158 |
| C | HOH723 |
| site_id | AG7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 612 |
| Chain | Residue |
| C | ASN110 |
| C | GLU111 |
| C | ARG112 |
| site_id | AG8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 613 |
| Chain | Residue |
| A | GLU58 |
| C | HIS46 |
| C | TYR266 |
| C | ARG267 |
| site_id | AG9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 614 |
| Chain | Residue |
| C | ASN385 |
| C | ARG387 |
| C | TYR425 |
| site_id | AH1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 615 |
| Chain | Residue |
| C | TYR280 |
| C | SO4601 |
| site_id | AH2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 617 |
| Chain | Residue |
| C | ASN229 |
| C | GLU311 |
| site_id | AH3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 618 |
| Chain | Residue |
| C | ARG32 |
| C | TYR33 |
| site_id | AH4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 619 |
| Chain | Residue |
| C | LYS31 |
| C | HOH765 |
| site_id | AH5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 620 |
| Chain | Residue |
| C | GLN87 |
| C | TYR165 |
| site_id | AH6 |
| Number of Residues | 13 |
| Details | binding site for residue SLU C 621 |
| Chain | Residue |
| C | HIS245 |
| C | PHE247 |
| C | THR251 |
| C | GLY316 |
| C | ALA317 |
| C | PRO318 |
| C | GLY339 |
| C | TYR340 |
| C | GLY341 |
| C | LEU342 |
| C | THR343 |
| C | ALA348 |
| C | ASP422 |
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 |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 128 |
| Chain | Residue | Details |
| C | ARG218 | electrostatic stabiliser |
| C | HIS245 | electrostatic stabiliser |
| C | THR343 | electrostatic stabiliser, hydrogen bond donor |
| C | LYS443 | electrostatic stabiliser, hydrogen bond donor |
| C | LYS529 | electrostatic stabiliser, hydrogen bond donor |
