Structure of PDB 1h6d Chain B

Receptor sequence

>1h6dB (length=381) Species: 542 (Zymomonas mobilis)

ATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILPG
FAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKID
AVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAANK
KLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQWR
LRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEVE
DRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQNL
ISVQTPGHANQSMMPQFIMPANNQFSAQLDHLAEAVINNKPVRSPGEEGM
QDVRLIQAIYEAARTGRPVNTDWGYVRQGGY

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): K181 Y269
• 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	B	G90 L91 G92 K93 Y94 S116 G117 K121 Y139 I157 L158 P159 N160 H163 E180 K181 R209 A248 W251 R252 Y269 Y348	G38 L39 G40 K41 Y42 S64 G65 K69 Y87 I105 L106 P107 N108 H111 E128 K129 R157 A196 W199 R200 Y217 Y296
BS02	GOL	B	K181 R252 D265 Y269	K129 R200 D213 Y217
BS03	NDP	B	P63 P66 A67 G68 R69	P11 P14 A15 G16 R17

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)