Structure of PDB 5epg Chain A

Receptor sequence

>5epgA (length=1288) Species: 9606 (Homo sapiens)

ASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACT
VMISRYNPITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQ
ERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTG
YRPIIDACKTFCKTPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTR
VFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPV
IISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMY
HALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSK
EGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKWEFVSAFRQAQRQ
ENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKLIGRH
WNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQIL
KKMDPVHYPSLADKYESALEDLHSHHCSTLKYQNPKQHPEDPIGHPIMHL
SGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPG
VVDIMTAEHLSDVNSFCKFLATDKVFCVGQLVCAVLADSEVQAKRAAKRV
KIVYQDLEPLILTIEESIQSFKPERKLEYGNVDEAFKVVDQILEGEIHMG
GQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTLKLPANKV
MCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGEDMLITG
GRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLSLFVIEMGLLKMDNAY
KFPNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPE
KVRIINMYKEIDQTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNA
ENYWKKKGLAMVPLKFPVGLGSRAAGQAAALVHIYLDGSVLVTHGGIEMG
QGVHTKMIQVVSRELRMPMSNVHLRGTSTETVPNANISGGSVVADLNGLA
VKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVGYFRGYESD
MNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPA
IDIGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTEL
HIALLPPSQNSNTLYSSKGLGELGVFLGCSVFFAIHDAVSAARQERGLHG
PLTLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNV

3D structure

• PDB: 5epg Optimization of the Expression of Human Aldehyde Oxidase for Investigations of Single-Nucleotide Polymorphisms.
• Chain: A
• Resolution: 3.39 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q776 V811 M889 K893 R921 G1269 E1270
• Catalytic site (residue number reindexed from 1): Q730 V765 M841 K845 R873 G1221 E1222
• 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	A	Q113 C114 G115 C117 C149 C151	Q110 C111 G112 C114 C146 C148
BS02	FES	A	G43 C44 G45 G47 C49 G50 C52 C74	G40 C41 G42 G44 C46 G47 C49 C71
BS03	FAD	A	G46 P263 V264 M266 G267 N268 T269 S270 V271 L344 A345 A353 S354 G357 H358 H363 S366 D367 L411 L438	G43 P229 V230 M232 G233 N234 T235 S236 V237 L310 A311 A319 S320 G323 H324 H329 S332 D333 L377 L404

Gene Ontology

Molecular Function

• GO:0004031 aldehyde oxidase activity
• GO:0005506 iron ion binding
• GO:0016491 oxidoreductase activity
• GO:0042802 identical protein 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:0006629 lipid metabolic process
• GO:0006805 xenobiotic metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:5epg, PDBe:5epg, PDBj:5epg
• PDBsum: 5epg
• PubMed: 26842593
• UniProt: Q06278|AOXA_HUMAN Aldehyde oxidase (Gene Name=AOX1)