Structure of PDB 1ofg Chain E

Receptor sequence

>1ofgE (length=381) Species: 542 (Zymomonas mobilis)

ATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILPG
FAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKID
AVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAANK
KLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQWR
LRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEVE
DRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQNL
ISVQTPGHANQSMMPQFIMPANNQFSAQLDHLAEAVINNKPVRSPGEEGM
QDVRLIQAIYEAARTGRPVNTDWGYVRQGGY

3D structure

• PDB: 1ofg The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
• Chain: E
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K129 Y217
• Catalytic site (residue number reindexed from 1): K129 Y217
• Enzyme Commision number: 1.1.99.28: glucose-fructose oxidoreductase.

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	NDP	E	L39 G40 K41 Y42 S64 G65 K69 Y87 I105 L106 P107 N108 H111 E128 K129 R157 A196 W199 R200 Y217	L39 G40 K41 Y42 S64 G65 K69 Y87 I105 L106 P107 N108 H111 E128 K129 R157 A196 W199 R200 Y217

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0016491 oxidoreductase activity
• GO:0047061 glucose-fructose oxidoreductase activity

Biological Process

• GO:0006061 sorbitol biosynthetic process

Cellular Component

• GO:0042597 periplasmic space

External links

• PDB: RCSB:1ofg, PDBe:1ofg, PDBj:1ofg
• PDBsum: 1ofg
• PubMed: 8994968
• UniProt: Q07982|GFO_ZYMMO Glucose--fructose oxidoreductase (Gene Name=gfo)