Structure of PDB 3zyv Chain D

Receptor sequence

>3zyvD (length=1257) Species: 10090 (Mus musculus)

SDELIFFVNGKKVTERNADPEVNLLFYLRKVIRLTGTKYGCGGGDCGACT
VMISRYDPISKRISHFSATACLVPICSLHGAAVTTVEGIGSTKTRIHPVQ
ERIAKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGNLCRCTG
YRPIVESAKSFCTKLYEKKEFQPLDPTQELIFPPELMRMAENTVLTFRGE
RTTWIAPGTLNDLLELKMKHPSAPLVIGNTYLGLHMKFTDVSYPIIISPA
RILELFVVTNTKQGLTLGTGLSLTQVKNVLSDVVSRLPKEKTQIYCALLK
QLKTLAGQQIRNVASLGGHIISRLPTSDLNPILGIGNCILNVASTEGIQQ
IPLNDHFLAILKPEQVLISVFVPRSSKWEFVSAFRQAPRQQNAFATVNAG
MKVVFKEDTNTITDLGILYGGIGATVISADKSCRQLIGRCWDEEMLDDAG
KMICEEVSLAPGGMEEYRKTLAISFLFMFYLDVLKQLKTRDISQKLLHIL
EDFPYGMQSFQDVDFQQPLQDPIGRPIMHQSGIKHATGEAVFCDDMSVLP
GELFLAVVTSSKSHAKIISLDASEALASLGVVDVVTARDVPGDNGEESLY
AQDEVICVGQIVCAVAADSYAHAQQAAKKVKIVYQDIPMIVTVQDALQYE
SFIGPERKLEQGNVEEAFQCADQILEGEVHLGGQEHFYMETQSVRVVPKG
EDKEMDIYVSSQDAAFTQEMVARTLGIPKNRINCHVKRVGGAFGGKASKP
GLLASVAAVAAQKTGRPIRFILERRDDMLITGGRHPLLGKYKIGFMNNGK
IKAADIQLYINGGCTPDDSELVIEYALLKLENAYKIPNLRVRGRVCKTNL
PSNTAFRGFGFPQGAFVTETCMSAVAAKCRPPEKVRELNMYRTIDRTIHN
QETNLLQCWEACVENSSYYNRKKAVDEFNQQRFWKKRGIAIIPMKFSVGF
PKTFYYQAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMS
YIHLDEMSTVTVPNTVTTGASTGADVNGRAVQNACQILMKRLEPIIKQNP
SGTWEEWVKEAFVQSISLSATGYFRGYQADMDWEKGEGDIFPYFVFGAAC
SEVEIDCLTGAHKNIRTDIVMDGSFSINPAVDIGQIEGAFVQGLGLYTLE
ELKYSPEGVLYTRGPHQYKIASVTDIPEEFHVSLLTPTPNPKAIYSSKGL
GEAGTFLGCSVFFAIAAAVAAAREERPIWAINSPATAEVIRMACEDQFTN
LPWSIPV

3D structure

• PDB: 3zyv The First Mammalian Aldehyde Oxidase Crystal Structure: Insights Into Substrate Specificity.
• Chain: D
• Resolution: 2.545 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q772 A807 Y885 K889 R917 G1265 E1266
• Catalytic site (residue number reindexed from 1): Q712 A747 Y825 K829 R857 G1201 E1202
• Enzyme Commision number: 1.17.3.-
  1.2.3.1: aldehyde 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	FES	D	C117 G118 C120 C152 C154	C111 G112 C114 C146 C148
BS02	FES	D	Y45 C47 G48 G50 C52 C55 T75 C77	Y39 C41 G42 G44 C46 C49 T69 C71
BS03	FAD	D	L264 I266 G267 N268 T269 Y270 T308 L344 A345 A353 S354 G357 H358 I360 S366 D367 V410 L411 F438	L225 I227 G228 N229 T230 Y231 T269 L305 A306 A314 S315 G318 H319 I321 S327 D328 V366 L367 F394

Gene Ontology

Molecular Function

• GO:0004031 aldehyde oxidase activity
• GO:0005506 iron ion binding
• GO:0009055 electron transfer activity
• GO:0016491 oxidoreductase activity
• GO:0030151 molybdenum ion binding
• GO:0042803 protein homodimerization activity
• GO:0043546 molybdopterin cofactor binding
• GO:0046872 metal ion binding
• GO:0050660 flavin adenine dinucleotide binding
• GO:0051287 NAD binding
• GO:0051536 iron-sulfur cluster binding
• GO:0051537 2 iron, 2 sulfur cluster binding
• GO:0071949 FAD binding

Biological Process

• GO:0006805 xenobiotic metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:3zyv, PDBe:3zyv, PDBj:3zyv
• PDBsum: 3zyv
• PubMed: 23019336
• UniProt: G3X982|AOXC_MOUSE Aldehyde oxidase 3 (Gene Name=Aox3)