Structure of PDB 4ynu Chain A

Receptor sequence

>4ynuA (length=569) Species: 332952 (Aspergillus flavus NRRL3357)

TTTYDYIVVGGGTSGLVVANRLSENPDVSVLLLEAGASVFNNPDVTNANG
YGLAFGSAIDWQYQSINQSYAGGKQQVLRAGKALGGTSTINGMAYTRAED
VQIDVWQKLGNEGWTWKDLLPYYLKSENLTAPTSSQVAAGAAYNPAVNGK
EGPLKVGWSGSLASGNLSVALNRTFQAAGVPWVEDVNGGKMRGFNIYPST
LDVDLNVREDAARAYYFPYDDRKNLHLLENTTANRLFWKNGSAEEAIADG
VEITSADGKVTRVHAKKEVIISAGALRSPLILELSGVGNPTILKKNNITP
RVDLPTVGENLQDQFNNGMAGEGYGVLAGASTVTYPSISDVFGNETDSIV
ASLRSQLSDYAAATVKVSNGHMKQEDLERLYQLQFDLIVKDKVPIAEILF
HPGGGNAVSSEFWGLLPFARGNIHISSNDPTAPAAINPNYFMFEWDGKSQ
AGIAKYIRKILRSAPLNKLIAKETKPGLSEIPATAADEKWVEWLKANYRS
NFHPVGTAAMMPRSIGGVVDNRLRVYGTSNVRVVDASVLPFQVCGHLVST
LYAVAERASDLIKEDAKSA

3D structure

• PDB: 4ynu Structural analysis of fungus-derived FAD glucose dehydrogenase
• Chain: A
• Resolution: 1.57 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V343 F414 W415 N503 H505 G547 H548
• Catalytic site (residue number reindexed from 1): V341 F412 W413 N501 H503 G545 H546
• Enzyme Commision number: 1.1.5.9: glucose 1-dehydrogenase (FAD, quinone).

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	A	G14 T15 S16 E36 A37 Y53 F57 W63 R81 G83 G88 T89 N93 G94 T234 A235 A275 G276 R279 F504 A538 H548 L549 V550 L553	G12 T13 S14 E34 A35 Y51 F55 W61 R79 G81 G86 T87 N91 G92 T232 A233 A273 G274 R277 F502 A536 H546 L547 V548 L551
BS02	LGC	A	Y53 E413 R501 N503 H505 H548	Y51 E411 R499 N501 H503 H546
BS03	LGC	A	A498 N499 R501	A496 N497 R499

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity
• GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
• GO:0050660 flavin adenine dinucleotide binding

External links

• PDB: RCSB:4ynu, PDBe:4ynu, PDBj:4ynu
• PDBsum: 4ynu
• PubMed: 26311535
• UniProt: B8MX95