5K3I
Crystal structure of Acyl-CoA oxidase-1 in Caenorhabditis elegans complexed with FAD and ATP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003997 | molecular_function | acyl-CoA oxidase activity |
A | 0005504 | molecular_function | fatty acid binding |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005777 | cellular_component | peroxisome |
A | 0005782 | cellular_component | peroxisomal matrix |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0009058 | biological_process | biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
A | 0042811 | biological_process | pheromone biosynthetic process |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0055088 | biological_process | lipid homeostasis |
A | 0071949 | molecular_function | FAD binding |
A | 1904070 | biological_process | ascaroside biosynthetic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003997 | molecular_function | acyl-CoA oxidase activity |
B | 0005504 | molecular_function | fatty acid binding |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005777 | cellular_component | peroxisome |
B | 0005782 | cellular_component | peroxisomal matrix |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0009058 | biological_process | biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
B | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
B | 0042811 | biological_process | pheromone biosynthetic process |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0055088 | biological_process | lipid homeostasis |
B | 0071949 | molecular_function | FAD binding |
B | 1904070 | biological_process | ascaroside biosynthetic process |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003997 | molecular_function | acyl-CoA oxidase activity |
C | 0005504 | molecular_function | fatty acid binding |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005777 | cellular_component | peroxisome |
C | 0005782 | cellular_component | peroxisomal matrix |
C | 0006629 | biological_process | lipid metabolic process |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0006635 | biological_process | fatty acid beta-oxidation |
C | 0009058 | biological_process | biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
C | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
C | 0042811 | biological_process | pheromone biosynthetic process |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0055088 | biological_process | lipid homeostasis |
C | 0071949 | molecular_function | FAD binding |
C | 1904070 | biological_process | ascaroside biosynthetic process |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003997 | molecular_function | acyl-CoA oxidase activity |
D | 0005504 | molecular_function | fatty acid binding |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005777 | cellular_component | peroxisome |
D | 0005782 | cellular_component | peroxisomal matrix |
D | 0006629 | biological_process | lipid metabolic process |
D | 0006631 | biological_process | fatty acid metabolic process |
D | 0006635 | biological_process | fatty acid beta-oxidation |
D | 0009058 | biological_process | biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
D | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
D | 0042811 | biological_process | pheromone biosynthetic process |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0055088 | biological_process | lipid homeostasis |
D | 0071949 | molecular_function | FAD binding |
D | 1904070 | biological_process | ascaroside biosynthetic process |
E | 0000166 | molecular_function | nucleotide binding |
E | 0003997 | molecular_function | acyl-CoA oxidase activity |
E | 0005504 | molecular_function | fatty acid binding |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005777 | cellular_component | peroxisome |
E | 0005782 | cellular_component | peroxisomal matrix |
E | 0006629 | biological_process | lipid metabolic process |
E | 0006631 | biological_process | fatty acid metabolic process |
E | 0006635 | biological_process | fatty acid beta-oxidation |
E | 0009058 | biological_process | biosynthetic process |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
E | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
E | 0042811 | biological_process | pheromone biosynthetic process |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0055088 | biological_process | lipid homeostasis |
E | 0071949 | molecular_function | FAD binding |
E | 1904070 | biological_process | ascaroside biosynthetic process |
F | 0000166 | molecular_function | nucleotide binding |
F | 0003997 | molecular_function | acyl-CoA oxidase activity |
F | 0005504 | molecular_function | fatty acid binding |
F | 0005515 | molecular_function | protein binding |
F | 0005524 | molecular_function | ATP binding |
F | 0005777 | cellular_component | peroxisome |
F | 0005782 | cellular_component | peroxisomal matrix |
F | 0006629 | biological_process | lipid metabolic process |
F | 0006631 | biological_process | fatty acid metabolic process |
F | 0006635 | biological_process | fatty acid beta-oxidation |
F | 0009058 | biological_process | biosynthetic process |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
F | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
F | 0042811 | biological_process | pheromone biosynthetic process |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0055088 | biological_process | lipid homeostasis |
F | 0071949 | molecular_function | FAD binding |
F | 1904070 | biological_process | ascaroside biosynthetic process |
G | 0000166 | molecular_function | nucleotide binding |
G | 0003997 | molecular_function | acyl-CoA oxidase activity |
G | 0005504 | molecular_function | fatty acid binding |
G | 0005515 | molecular_function | protein binding |
G | 0005524 | molecular_function | ATP binding |
G | 0005777 | cellular_component | peroxisome |
G | 0005782 | cellular_component | peroxisomal matrix |
G | 0006629 | biological_process | lipid metabolic process |
G | 0006631 | biological_process | fatty acid metabolic process |
G | 0006635 | biological_process | fatty acid beta-oxidation |
G | 0009058 | biological_process | biosynthetic process |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
G | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
G | 0042811 | biological_process | pheromone biosynthetic process |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
G | 0055088 | biological_process | lipid homeostasis |
G | 0071949 | molecular_function | FAD binding |
G | 1904070 | biological_process | ascaroside biosynthetic process |
H | 0000166 | molecular_function | nucleotide binding |
H | 0003997 | molecular_function | acyl-CoA oxidase activity |
H | 0005504 | molecular_function | fatty acid binding |
H | 0005515 | molecular_function | protein binding |
H | 0005524 | molecular_function | ATP binding |
H | 0005777 | cellular_component | peroxisome |
H | 0005782 | cellular_component | peroxisomal matrix |
H | 0006629 | biological_process | lipid metabolic process |
H | 0006631 | biological_process | fatty acid metabolic process |
H | 0006635 | biological_process | fatty acid beta-oxidation |
H | 0009058 | biological_process | biosynthetic process |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
H | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
H | 0042811 | biological_process | pheromone biosynthetic process |
H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
H | 0055088 | biological_process | lipid homeostasis |
H | 0071949 | molecular_function | FAD binding |
H | 1904070 | biological_process | ascaroside biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | binding site for residue FAD A 701 |
Chain | Residue |
A | LEU115 |
A | THR432 |
A | GLU436 |
A | MET438 |
A | VAL439 |
B | ARG320 |
B | GLN322 |
B | VAL334 |
B | TYR337 |
B | THR339 |
B | GLN340 |
A | TYR149 |
B | ARG343 |
B | ALA408 |
B | GLY410 |
B | GLY411 |
B | TYR414 |
B | HOH803 |
A | GLN151 |
A | THR152 |
A | GLY157 |
A | THR158 |
A | TRP189 |
A | PRO190 |
A | GLY191 |
site_id | AC2 |
Number of Residues | 16 |
Details | binding site for residue ATP A 702 |
Chain | Residue |
A | SER392 |
A | HIS396 |
A | ASN437 |
A | MET438 |
A | ARG533 |
A | ARG536 |
A | TYR581 |
A | HOH839 |
A | HOH847 |
A | HOH848 |
B | HIS342 |
B | ARG343 |
B | GLN404 |
B | TYR573 |
B | MG701 |
B | HOH814 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue MG A 703 |
Chain | Residue |
A | ASP577 |
B | ATP703 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue MG B 701 |
Chain | Residue |
A | ATP702 |
A | HOH839 |
B | ASP577 |
site_id | AC5 |
Number of Residues | 24 |
Details | binding site for residue FAD B 702 |
Chain | Residue |
A | ARG320 |
A | GLN322 |
A | VAL334 |
A | TYR337 |
A | THR339 |
A | GLN340 |
A | ARG343 |
A | ALA408 |
A | GLY410 |
A | GLY411 |
A | TYR414 |
B | LEU115 |
B | TYR149 |
B | GLN151 |
B | THR152 |
B | GLY157 |
B | THR158 |
B | TRP189 |
B | GLY191 |
B | THR432 |
B | GLU436 |
B | MET438 |
B | VAL439 |
B | HOH807 |
site_id | AC6 |
Number of Residues | 14 |
Details | binding site for residue ATP B 703 |
Chain | Residue |
A | HIS342 |
A | ARG343 |
A | GLN404 |
A | TYR573 |
A | MG703 |
B | SER392 |
B | HIS396 |
B | ASN437 |
B | MET438 |
B | LEU441 |
B | ARG533 |
B | ARG536 |
B | TYR581 |
B | HOH864 |
site_id | AC7 |
Number of Residues | 27 |
Details | binding site for residue FAD C 701 |
Chain | Residue |
C | HOH824 |
C | HOH848 |
D | ARG320 |
D | GLN322 |
D | VAL334 |
D | TYR337 |
D | GLN340 |
D | ARG343 |
D | ALA408 |
D | GLY410 |
D | GLY411 |
D | TYR414 |
C | LEU115 |
C | TYR149 |
C | GLN151 |
C | THR152 |
C | GLY157 |
C | THR158 |
C | TRP189 |
C | PRO190 |
C | GLY191 |
C | THR432 |
C | GLU436 |
C | MET438 |
C | VAL439 |
C | HOH806 |
C | HOH821 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue MG C 702 |
Chain | Residue |
C | ASP577 |
D | ATP801 |
D | HOH935 |
site_id | AC9 |
Number of Residues | 15 |
Details | binding site for residue ATP C 703 |
Chain | Residue |
C | SER392 |
C | HIS396 |
C | ASN437 |
C | MET438 |
C | LEU441 |
C | ARG533 |
C | ARG536 |
C | TYR581 |
C | HOH811 |
D | HIS342 |
D | ARG343 |
D | GLN404 |
D | TYR573 |
D | MG802 |
D | HOH916 |
site_id | AD1 |
Number of Residues | 14 |
Details | binding site for residue ATP D 801 |
Chain | Residue |
C | HIS342 |
C | GLN404 |
C | TYR573 |
C | MG702 |
D | SER392 |
D | HIS396 |
D | ASN437 |
D | MET438 |
D | LEU441 |
D | ARG533 |
D | ARG536 |
D | TYR581 |
D | HOH931 |
D | HOH935 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue MG D 802 |
Chain | Residue |
C | ARG533 |
C | ATP703 |
site_id | AD3 |
Number of Residues | 25 |
Details | binding site for residue FAD D 803 |
Chain | Residue |
C | ARG320 |
C | GLN322 |
C | VAL334 |
C | TYR337 |
C | THR339 |
C | GLN340 |
C | ARG343 |
C | ALA408 |
C | GLY410 |
C | GLY411 |
D | LEU115 |
D | TYR149 |
D | GLN151 |
D | THR152 |
D | GLY157 |
D | THR158 |
D | TRP189 |
D | PRO190 |
D | GLY191 |
D | THR432 |
D | TYR433 |
D | GLU436 |
D | MET438 |
D | VAL439 |
D | HOH903 |
site_id | AD4 |
Number of Residues | 24 |
Details | binding site for residue FAD E 701 |
Chain | Residue |
E | LEU115 |
E | TYR149 |
E | GLN151 |
E | THR152 |
E | GLY157 |
E | THR158 |
E | TRP189 |
E | PRO190 |
E | GLY191 |
E | THR432 |
E | GLU436 |
E | MET438 |
E | VAL439 |
F | ARG320 |
F | GLN322 |
F | VAL334 |
F | TYR337 |
F | GLN340 |
F | ARG343 |
F | ALA408 |
F | GLY410 |
F | GLY411 |
F | TYR414 |
F | HOH804 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue MG E 702 |
Chain | Residue |
E | ASP577 |
E | HOH839 |
F | ATP702 |
site_id | AD6 |
Number of Residues | 15 |
Details | binding site for residue ATP E 703 |
Chain | Residue |
E | SER392 |
E | HIS396 |
E | ASN437 |
E | MET438 |
E | ARG533 |
E | ARG536 |
E | TYR581 |
E | HOH801 |
E | HOH823 |
E | HOH828 |
F | HIS342 |
F | ARG343 |
F | GLN404 |
F | TYR573 |
F | MG703 |
site_id | AD7 |
Number of Residues | 23 |
Details | binding site for residue FAD F 701 |
Chain | Residue |
E | ARG320 |
E | GLN322 |
E | VAL334 |
E | TYR337 |
E | GLN340 |
E | ARG343 |
E | ALA408 |
E | GLY410 |
E | GLY411 |
E | TYR414 |
E | HOH826 |
F | LEU115 |
F | TYR149 |
F | GLN151 |
F | THR152 |
F | GLY157 |
F | THR158 |
F | TRP189 |
F | THR432 |
F | GLU436 |
F | MET438 |
F | VAL439 |
F | HOH803 |
site_id | AD8 |
Number of Residues | 11 |
Details | binding site for residue ATP F 702 |
Chain | Residue |
E | HIS342 |
E | GLN404 |
E | TYR573 |
E | MG702 |
F | SER392 |
F | HIS396 |
F | ASN437 |
F | MET438 |
F | ARG533 |
F | ARG536 |
F | TYR581 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue MG F 703 |
Chain | Residue |
E | ATP703 |
F | ASP577 |
site_id | AE1 |
Number of Residues | 24 |
Details | binding site for residue FAD G 701 |
Chain | Residue |
G | LEU115 |
G | TYR149 |
G | GLN151 |
G | THR152 |
G | GLY157 |
G | THR158 |
G | TRP189 |
G | PRO190 |
G | GLY191 |
G | THR432 |
G | GLU436 |
G | MET438 |
G | VAL439 |
G | HOH819 |
H | ARG320 |
H | GLN322 |
H | VAL334 |
H | TYR337 |
H | GLN340 |
H | ARG343 |
H | ALA408 |
H | GLY410 |
H | GLY411 |
H | TYR414 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue MG G 702 |
Chain | Residue |
G | ASP577 |
H | ATP702 |
site_id | AE3 |
Number of Residues | 13 |
Details | binding site for residue ATP G 703 |
Chain | Residue |
G | SER392 |
G | HIS396 |
G | ASN437 |
G | MET438 |
G | LEU441 |
G | ARG533 |
G | ARG536 |
G | TYR581 |
H | HIS342 |
H | ARG343 |
H | GLN404 |
H | TYR573 |
H | MG703 |
site_id | AE4 |
Number of Residues | 29 |
Details | binding site for residue FAD H 701 |
Chain | Residue |
G | ARG320 |
G | GLN322 |
G | VAL334 |
G | TYR337 |
G | THR339 |
G | GLN340 |
G | ARG343 |
G | ALA408 |
G | GLY410 |
G | GLY411 |
G | TYR414 |
G | HOH837 |
H | LEU115 |
H | TYR149 |
H | GLN151 |
H | THR152 |
H | GLY157 |
H | THR158 |
H | TRP189 |
H | PRO190 |
H | GLY191 |
H | THR432 |
H | GLU436 |
H | MET438 |
H | VAL439 |
H | HOH803 |
H | HOH835 |
H | HOH849 |
H | HOH858 |
site_id | AE5 |
Number of Residues | 12 |
Details | binding site for residue ATP H 702 |
Chain | Residue |
G | HIS342 |
G | ARG343 |
G | GLN404 |
G | TYR573 |
G | MG702 |
H | SER392 |
H | HIS396 |
H | ASN437 |
H | MET438 |
H | ARG533 |
H | ARG536 |
H | TYR581 |
site_id | AE6 |
Number of Residues | 2 |
Details | binding site for residue MG H 703 |
Chain | Residue |
G | ATP703 |
H | ASP577 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PIRSR:PIRSR000168-1 |
Chain | Residue | Details |
A | ALA434 | |
B | ALA434 | |
C | ALA434 | |
D | ALA434 | |
E | ALA434 | |
F | ALA434 | |
G | ALA434 | |
H | ALA434 |
site_id | SWS_FT_FI2 |
Number of Residues | 48 |
Details | BINDING: in other chain => ECO:0000269|PubMed:27551084, ECO:0007744|PDB:5K3I |
Chain | Residue | Details |
A | TYR149 | |
B | HIS396 | |
B | ARG533 | |
B | TYR581 | |
C | TYR149 | |
C | GLY157 | |
C | SER392 | |
C | HIS396 | |
C | ARG533 | |
C | TYR581 | |
D | TYR149 | |
A | GLY157 | |
D | GLY157 | |
D | SER392 | |
D | HIS396 | |
D | ARG533 | |
D | TYR581 | |
E | TYR149 | |
E | GLY157 | |
E | SER392 | |
E | HIS396 | |
E | ARG533 | |
A | SER392 | |
E | TYR581 | |
F | TYR149 | |
F | GLY157 | |
F | SER392 | |
F | HIS396 | |
F | ARG533 | |
F | TYR581 | |
G | TYR149 | |
G | GLY157 | |
G | SER392 | |
A | HIS396 | |
G | HIS396 | |
G | ARG533 | |
G | TYR581 | |
H | TYR149 | |
H | GLY157 | |
H | SER392 | |
H | HIS396 | |
H | ARG533 | |
H | TYR581 | |
A | ARG533 | |
A | TYR581 | |
B | TYR149 | |
B | GLY157 | |
B | SER392 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: in other chain => ECO:0000255|PIRSR:PIRSR000168-2, ECO:0000269|PubMed:27551084, ECO:0007744|PDB:5K3I |
Chain | Residue | Details |
A | GLY191 | |
B | GLY191 | |
C | GLY191 | |
D | GLY191 | |
E | GLY191 | |
F | GLY191 | |
G | GLY191 | |
H | GLY191 |
site_id | SWS_FT_FI4 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O62137 |
Chain | Residue | Details |
A | LYS285 | |
B | TYR433 | |
C | LYS285 | |
C | ARG295 | |
C | HIS342 | |
C | GLY411 | |
C | TYR433 | |
D | LYS285 | |
D | ARG295 | |
D | HIS342 | |
D | GLY411 | |
A | ARG295 | |
D | TYR433 | |
E | LYS285 | |
E | ARG295 | |
E | HIS342 | |
E | GLY411 | |
E | TYR433 | |
F | LYS285 | |
F | ARG295 | |
F | HIS342 | |
F | GLY411 | |
A | HIS342 | |
F | TYR433 | |
G | LYS285 | |
G | ARG295 | |
G | HIS342 | |
G | GLY411 | |
G | TYR433 | |
H | LYS285 | |
H | ARG295 | |
H | HIS342 | |
H | GLY411 | |
A | GLY411 | |
H | TYR433 | |
A | TYR433 | |
B | LYS285 | |
B | ARG295 | |
B | HIS342 | |
B | GLY411 |
site_id | SWS_FT_FI5 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27551084, ECO:0007744|PDB:5K3I |
Chain | Residue | Details |
A | ARG320 | |
D | ARG320 | |
D | GLN340 | |
D | GLN404 | |
E | ARG320 | |
E | GLN340 | |
E | GLN404 | |
F | ARG320 | |
F | GLN340 | |
F | GLN404 | |
G | ARG320 | |
A | GLN340 | |
G | GLN340 | |
G | GLN404 | |
H | ARG320 | |
H | GLN340 | |
H | GLN404 | |
A | GLN404 | |
B | ARG320 | |
B | GLN340 | |
B | GLN404 | |
C | ARG320 | |
C | GLN340 | |
C | GLN404 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:O62137 |
Chain | Residue | Details |
A | GLU436 | |
B | GLU436 | |
C | GLU436 | |
D | GLU436 | |
E | GLU436 | |
F | GLU436 | |
G | GLU436 | |
H | GLU436 |