5K3J
Crystals structure of Acyl-CoA oxidase-2 in Caenorhabditis elegans bound with FAD, ascaroside-CoA, and ATP
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 | 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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | binding site for residue FAD A 701 |
Chain | Residue |
A | LEU113 |
A | THR430 |
A | GLU434 |
A | MET436 |
A | VAL437 |
A | 6QA703 |
A | HOH801 |
A | HOH833 |
B | ARG318 |
B | GLN320 |
B | VAL332 |
A | TYR147 |
B | TYR335 |
B | THR337 |
B | GLN338 |
B | ARG341 |
B | ALA406 |
B | GLY408 |
B | GLY409 |
B | HOH816 |
B | HOH861 |
A | GLN149 |
A | THR150 |
A | GLY155 |
A | SER156 |
A | TRP187 |
A | PRO188 |
A | GLY189 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue ATP A 702 |
Chain | Residue |
A | SER390 |
A | HIS394 |
A | ASN435 |
A | MET436 |
A | LEU439 |
A | ARG525 |
A | ARG528 |
A | TYR573 |
A | HOH828 |
B | HIS340 |
B | ARG341 |
B | GLN402 |
B | TYR565 |
B | MG701 |
B | HOH842 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue 6QA A 703 |
Chain | Residue |
A | LEU117 |
A | TYR147 |
A | GLN149 |
A | GLY155 |
A | SER156 |
A | LEU158 |
A | ARG159 |
A | PHE243 |
A | HIS281 |
A | LYS283 |
A | TYR286 |
A | MET289 |
A | ARG293 |
A | GLU299 |
A | HIS382 |
A | TYR431 |
A | ALA432 |
A | GLY433 |
A | VAL437 |
A | GLN441 |
A | ARG444 |
A | FAD701 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue MG B 701 |
Chain | Residue |
A | ATP702 |
B | ASP569 |
site_id | AC5 |
Number of Residues | 25 |
Details | binding site for residue FAD B 702 |
Chain | Residue |
A | ARG318 |
A | VAL332 |
A | TYR335 |
A | THR337 |
A | GLN338 |
A | ARG341 |
A | ALA406 |
A | GLY408 |
A | GLY409 |
B | LEU113 |
B | TYR147 |
B | GLN149 |
B | THR150 |
B | GLY155 |
B | SER156 |
B | TRP187 |
B | PRO188 |
B | GLY189 |
B | THR430 |
B | GLY433 |
B | GLU434 |
B | MET436 |
B | VAL437 |
B | 6QA705 |
B | HOH832 |
site_id | AC6 |
Number of Residues | 17 |
Details | binding site for residue ATP B 703 |
Chain | Residue |
B | ASN435 |
B | MET436 |
B | LEU439 |
B | ARG525 |
B | ARG528 |
B | TYR573 |
B | MG704 |
B | HOH808 |
B | HOH813 |
B | HOH844 |
A | HIS340 |
A | ARG341 |
A | GLN402 |
A | TYR565 |
A | ASP569 |
B | SER390 |
B | HIS394 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue MG B 704 |
Chain | Residue |
B | ATP703 |
site_id | AC8 |
Number of Residues | 23 |
Details | binding site for residue 6QA B 705 |
Chain | Residue |
B | ALA116 |
B | LEU117 |
B | GLN149 |
B | GLY155 |
B | SER156 |
B | LEU158 |
B | ARG159 |
B | PHE243 |
B | LYS283 |
B | TYR286 |
B | MET289 |
B | ARG293 |
B | GLU299 |
B | HIS382 |
B | TYR431 |
B | ALA432 |
B | GLY433 |
B | VAL437 |
B | MET438 |
B | GLN441 |
B | ARG444 |
B | LYS448 |
B | FAD702 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PIRSR:PIRSR000168-1 |
Chain | Residue | Details |
A | ALA432 | |
B | ALA432 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: in other chain => ECO:0000269|PubMed:27551084, ECO:0007744|PDB:5K3J |
Chain | Residue | Details |
A | TYR147 | |
B | TYR573 | |
A | GLY155 | |
A | GLU434 | |
A | ARG525 | |
A | TYR573 | |
B | TYR147 | |
B | GLY155 | |
B | GLU434 | |
B | ARG525 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: in other chain => ECO:0000255|PIRSR:PIRSR000168-2, ECO:0000269|PubMed:27551084, ECO:0007744|PDB:5K3J |
Chain | Residue | Details |
A | GLY189 | |
B | GLY189 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27551084, ECO:0007744|PDB:5K3J |
Chain | Residue | Details |
A | LYS283 | |
B | ARG293 | |
B | ARG318 | |
B | GLN338 | |
B | HIS340 | |
B | GLN402 | |
B | GLY409 | |
B | TYR431 | |
A | ARG293 | |
A | ARG318 | |
A | GLN338 | |
A | HIS340 | |
A | GLN402 | |
A | GLY409 | |
A | TYR431 | |
B | LYS283 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:O62140 |
Chain | Residue | Details |
A | SER390 | |
A | HIS394 | |
B | SER390 | |
B | HIS394 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Important for asc-omega-C5-CoA binding and thus substrate specificity => ECO:0000269|PubMed:27551084, ECO:0000312|PDB:5K3J |
Chain | Residue | Details |
A | GLU299 | |
B | GLU299 |