Structure of PDB 6q6q Chain A

Receptor sequence

>6q6qA (length=1292) Species: 9606 (Homo sapiens)

ASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACT
VMISRYNPITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQ
ERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTG
YRPIIDACKTFCKTPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTR
VFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPV
IISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMY
HALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSK
EGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKWEFVSAFRQAQRQ
ENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKLIGRH
WNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQIL
KKMDPVHYPSLADKYESALEDLHSHHCSTLKYQNPKQHPEDPIGHPIMHL
SGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPG
VVDIMTAEHLSDVNSFCFFTEAEKFLATDKVFCVGQLVCAVLADSEVQAK
RAAKRVKIVYQDLEPLILTIEESIQHSFKPERKLEYGNVDEAFKVVDQIL
EGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTL
KLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERG
EDMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLSLFVIEMGL
LKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAA
KCGLSPEKVRIINMYKEIDQTPYKQEINAKNLIQCWRECMAMSSYSLRKV
AVEKFNAENYWKKKGLAMVPLKFPVGLGSRAAGQAAALVHIYLDGSVLVT
HGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETVPNANISGGSVV
ADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVGY
FRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDV
GCSINPAIDIGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAI
CDMPTELHIALLPPSNTLYSSKGLRESGVFLGCSVFFAIHDAVSAARQER
GLHGPLTLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNV

3D structure

• PDB: 6q6q Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms.
• Chain: A
• Resolution: 3.10004 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q776 V811 M889 K893 R921 R1269 E1270
• Catalytic site (residue number reindexed from 1): Q737 V772 M848 K852 R880 R1225 E1226
• 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 C117 C149 C151	Q110 C111 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 G47 G48 P263 V264 I265 M266 G267 N268 T269 S270 V271 L344 A345 I349 A353 S354 G357 H358 I360 S361 H363 S366 D367 L411 L438	G43 G44 G45 P229 V230 I231 M232 G233 N234 T235 S236 V237 L310 A311 I315 A319 S320 G323 H324 I326 S327 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:6q6q, PDBe:6q6q, PDBj:6q6q
• PDBsum: 6q6q
• PubMed: 30985987
• UniProt: Q06278|AOXA_HUMAN Aldehyde oxidase (Gene Name=AOX1)