Structure of PDB 1h6d Chain A

Receptor sequence

>1h6dA (length=383) Species: 542 (Zymomonas mobilis)

QAATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQIL
PGFAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPK
IDAVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAA
NKKLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQ
WRLRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVE
VEDRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQ
NLISVQTPGHANQSMMPQFIMPANNQFSAQLDHLAEAVINNKPVRSPGEE
GMQDVRLIQAIYEAARTGRPVNTDWGYVRQGGY

3D structure

• PDB: 1h6d Crystal Structures of the Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas Mobilis and its Complexes with Bound Ligands
• Chain: A
• Resolution: 2.05 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K181 Y269
• Catalytic site (residue number reindexed from 1): K131 Y219
• 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	A	G90 L91 G92 K93 Y94 S116 G117 K121 Y139 I157 L158 P159 N160 H163 E180 K181 R209 A248 W251 R252 Y269 Y348	G40 L41 G42 K43 Y44 S66 G67 K71 Y89 I107 L108 P109 N110 H113 E130 K131 R159 A198 W201 R202 Y219 Y298
BS02	GOL	A	K181 R252 D265 Y269	K131 R202 D215 Y219
BS03	NDP	A	A67 G68 R69	A17 G18 R19

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding

External links

• PDB: RCSB:1h6d, PDBe:1h6d, PDBj:1h6d
• PDBsum: 1h6d
• PubMed: 11705375
• UniProt: Q07982|GFO_ZYMMO Glucose--fructose oxidoreductase (Gene Name=gfo)