Structure of PDB 1h6d Chain C

Receptor sequence

>1h6dC (length=382) Species: 542 (Zymomonas mobilis)

AATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILP
GFAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKI
DAVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAAN
KKLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQW
RLRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEV
EDRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQN
LISVQTPGHANQSMMPQFIMPANNQFSAQLDHLAEAVINNKPVRSPGEEG
MQDVRLIQAIYEAARTGRPVNTDWGYVRQGGY

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): K181 Y269
• Catalytic site (residue number reindexed from 1): K130 Y218
• 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	C	P66 A67 G68 R69	P15 A16 G17 R18
BS02	NDP	C	G90 L91 G92 K93 Y94 S116 G117 K121 Y139 I157 L158 P159 N160 H163 E180 K181 R209 A248 W251 R252 Y269 Y348	G39 L40 G41 K42 Y43 S65 G66 K70 Y88 I106 L107 P108 N109 H112 E129 K130 R158 A197 W200 R201 Y218 Y297
BS03	GOL	C	K181 R252 D265 Y269	K130 R201 D214 Y218

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)