Structure of PDB 6a2u Chain D

Receptor sequence

>6a2uD (length=530) Species: 292 (Burkholderia cepacia)

DVVVVGSGVAGAIVAHQLAMAGKAVILLEAGPRMPRWEIVERFRNQPDKM
DFMAPYPSSPWAPHPEYGPPNDYLILKGEHKFNSQYIRAVGGTTWHWAAS
AWRFIPNDFKMKSVYGVGRDWPIQYDDLEPYYQRAEEELGVWGPGPEEDL
YSPRKQPYPMPPLPLSFNEQTIKTALNNYDPKFHVVTEPVARNSRPYDGR
PTCCGNNNCMPICPIGAMYNGIVHVEKAERAGAKLIENAVVYKLETGPDK
RIVAALYKDKTGAEHRVEGKYFVLAANGIETPKILLMSANRDFPNGVANS
SDMVGRNLMDHPGTGVSFYASEKLWPGRGPQEMTSLIGFRDGPFRATEAA
KKIHLSNLSRIDQETQKIFKAGKLMKPDELDAQIRDRSARYVQFDCFHEI
LPQPENRIVPSKTATDAIGIPRPEITYAIDDYVKRGAAHTREVYATAAKV
LGGTDVVFNDEFAPNNHITGSTIMGADARDSVVDKDCRTFDHPNLFISSS
ATMPTVGTVNVTLTIAALALRMSDTLKKEV

3D structure

• PDB: 6a2u X-ray structure of the direct electron transfer-type FAD glucose dehydrogenase catalytic subunit complexed with a hitchhiker protein.
• Chain: D
• Resolution: 2.6 Å

Enzymatic activity

• 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	D	G15 G17 V18 A19 E38 A39 Q94 R97 G101 T102 T103 H105 W106 A107 S109 M219 V250 A285 E289 N475 N519 T521	G6 G8 V9 A10 E29 A30 Q85 R88 G92 T93 T94 H96 W97 A98 S100 M210 V241 A276 E280 N466 N510 T512
BS02	F3S	D	C212 C213 N215 N217 C218 C222 I224 P339	C203 C204 N206 N208 C209 C213 I215 P330

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0016491 oxidoreductase activity
• GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
• GO:0046872 metal ion binding
• GO:0050660 flavin adenine dinucleotide binding
• GO:0051538 3 iron, 4 sulfur cluster binding

External links

• PDB: RCSB:6a2u, PDBe:6a2u, PDBj:6a2u
• PDBsum: 6a2u
• PubMed: 31478907
• UniProt: Q8GQE7