Structure of PDB 2vft Chain A

Receptor sequence

>2vftA (length=415) Species: 100226 (Streptomyces coelicolor A3(2))

DITVTNWAGNITYTAKELLRPHSLDALRALVADSARVRVLGSGHSFNEIA
EPGDGGVLLSLAGLPSVVDVDTAARTVRVGGGVRYAELARVVHARGLALP
NMASLPHISVAGSVATGTHGSGVGNGSLASVVREVELVTADGSTVVIARG
DERFGGAVTSLGALGVVTSLTLDLEPAYEMEQHVFTELPLAGLDPATFET
VMAAAYSVSLFTDWRAPGFRQVWLKRRTDRPLDGFPYAAPAAEKMHPVPG
MPAVNCTEQFGVPGPWHERLPHFRAEFTPSSGAELQSEYLMPREHALAAL
HAMDAIRETLAPVLQTCEIRTVAADAQWLSPAYGRDTVAAHFTWVEDTAA
VLPVVRRLEEALVPFAARPHWGKVFTVPAGELRALYPRLADFGALAGALD
PAGKFTNAFVRGVLA

3D structure

• PDB: 2vft Structural Analysis of the Catalytic Mechanism and Stereoselectivity in Streptomyces Coelicolor Alditol Oxidase.
• Chain: A
• Resolution: 1.6 Å

Enzymatic activity

• Enzyme Commision number: 1.1.3.41: alditol 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	FAD	A	W9 V41 G43 S44 G45 H46 S47 I51 A105 S106 I110 A113 G114 T118 T120 H121 G164 V169 Q288 R322 H372 K375	W7 V39 G41 S42 G43 H44 S45 I49 A103 S104 I108 A111 G112 T116 T118 H119 G162 V167 Q286 R320 H370 K373
BS02	SOR	A	S106 E320 R322 H343 T345 K375	S104 E318 R320 H341 T343 K373

Gene Ontology

Molecular Function

• GO:0003885 D-arabinono-1,4-lactone oxidase activity
• GO:0016491 oxidoreductase activity
• GO:0016899 oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor
• GO:0050582 xylitol oxidase activity
• GO:0050660 flavin adenine dinucleotide binding
• GO:0071949 FAD binding
• GO:0080049 L-gulono-1,4-lactone dehydrogenase activity

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:2vft, PDBe:2vft, PDBj:2vft
• PDBsum: 2vft
• PubMed: 18154360
• UniProt: Q9ZBU1|XYOA_STRCO Alditol oxidase (Gene Name=xyoA)