Structure of PDB 5k3i Chain B

Receptor sequence
>5k3iB (length=657) Species: 6239 (Caenorhabditis elegans) [Search protein sequence]
VHLNKTIQEGDNPDLTAERLTATFDTHAMAAQIYGGEMRARRRREITAKL
AEIPELHDSMPLPYMTREEKIMESARKLTVLTQRMSEIIDPTDAGELYHL
NNEVLGIEGNPMALHGVMFIPALNAQASDEQQAKWLIRALRREIIGTYAQ
TEMGHGTNLQNLETTATYDIGTQEFVLHTPKITALKWWPGNLGKSSNYAV
VVAHMYIKGKNFGPHTFMVPLRDEKTHKPLPGITIGDIGPKMAYNIVDNG
FLGFNNYRIPRTNLLMRHTKVEADGTYIKPPAMVHVRSYMLTGQAIMLSY
ALNIATRYSAVRRQGQIDKNEPEVKVLEYQTQQHRLFPFIARAYAFQFAG
AETVKLYERVLKEMKSLMADLHALTSGLKSVVTHQTGEGIEQARMACGGH
GYSMASYISEIYGVAIGGCTYAGENMVMLLQLARYLVKSAALVKSGKASQ
LGPLVAYLGARSEPTSLIDRVPNGGITEYIKTFQHIAKRQTLKAANKFFG
LMENGEKREIAWNKSSVELNRASRLHTRLFIVEAFARRVNEIGDITIKEA
LSDLLHLHVNYELLDVATYALEDGFMSSTQLDYVRDQLYFYLQKIRPNAV
SLLDSWEFSDRELRSVLGRRDGHVYENLFKWAKESPLNKTDVLPSVDTYL
KPMMEKA
3D structure
PDB5k3i Structural characterization of acyl-CoA oxidases reveals a direct link between pheromone biosynthesis and metabolic state in Caenorhabditis elegans.
ChainB
Resolution2.683 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.3.3.-
1.3.3.6: acyl-CoA oxidase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 FAD B R320 Y337 Q340 R343 A408 G411 Y414 R312 Y329 Q332 R335 A396 G399 Y402
BS02 ATP B H342 Q404 Y573 H334 Q392 Y561
BS03 FAD B Q151 T152 G157 T158 W189 T432 E436 V439 Q150 T151 G156 T157 W188 T420 E424 V427
BS04 ATP B S392 H396 N437 M438 R533 R536 Y581 S380 H384 N425 M426 R521 R524 Y569
Gene Ontology
Molecular Function
GO:0003997 acyl-CoA oxidase activity
GO:0005504 fatty acid binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0009058 biosynthetic process
GO:0033540 fatty acid beta-oxidation using acyl-CoA oxidase
GO:0042811 pheromone biosynthetic process
GO:0055088 lipid homeostasis
GO:1904070 ascaroside biosynthetic process
Cellular Component
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5k3i, PDBe:5k3i, PDBj:5k3i
PDBsum5k3i
PubMed27551084
UniProtO62140|ACX11_CAEEL Acyl-coenzyme A oxidase acox-1.1 (Gene Name=acox-1.1)

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