Structure of PDB 2vfu Chain A

Receptor sequence

>2vfuA (length=414) Species: 100226 (Streptomyces coelicolor A3(2))

ITVTNWAGNITYTAKELLRPHSLDALRALVADSARVRVLGSGHSFNEIAE
PGDGGVLLSLAGLPSVVDVDTAARTVRVGGGVRYAELARVVHARGLALPN
MASLPHISVAGSVATGTHGSGVGNGSLASVVREVELVTADGSTVVIARGD
ERFGGAVTSLGALGVVTSLTLDLEPAYEMEQHVFTELPLAGLDPATFETV
MAAAYSVSLFTDWRAPGFRQVWLKRRTDRPLDGFPYAAPAAEKMHPVPGM
PAVNCTEQFGVPGPWHERLPHFRAEFTPSSGAELQSEYLMPREHALAALH
AMDAIRETLAPVLQTCEIRTVAADAQWLSPAYGRDTVAAHFTWVEDTAAV
LPVVRRLEEALVPFAARPHWGKVFTVPAGELRALYPRLADFGALAGALDP
AGKFTNAFVRGVLA

3D structure

• PDB: 2vfu Structural Analysis of the Catalytic Mechanism and Stereoselectivity in Streptomyces Coelicolor Alditol Oxidase.
• Chain: A
• Resolution: 1.9 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 F48 A105 S106 I110 S111 A113 G114 T118 T120 H121 G164 V169 Q288 R322 H372 K375	W6 V38 G40 S41 G42 H43 S44 F45 A102 S103 I107 S108 A110 G111 T115 T117 H118 G161 V166 Q285 R319 H369 K372
BS02	MTL	A	S106 F275 E320 H343 T345 K375	S103 F272 E317 H340 T342 K372

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