Structure of PDB 1h6d Chain J

Receptor sequence
>1h6dJ (length=381) Species: 542 (Zymomonas mobilis) [Search protein sequence]
ATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILPG
FAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKID
AVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAANK
KLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQWR
LRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEVE
DRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQNL
ISVQTPGHANQSMMPQFIMPANNQFSAQLDHLAEAVINNKPVRSPGEEGM
QDVRLIQAIYEAARTGRPVNTDWGYVRQGGY
3D structure
PDB1h6d Crystal Structures of the Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas Mobilis and its Complexes with Bound Ligands
ChainJ
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 J 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 J R252 D265 Y269 R200 D213 Y217
BS03 NDP J A67 R69 A15 R17
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding

View graph for
Molecular Function
External links
PDB RCSB:1h6d, PDBe:1h6d, PDBj:1h6d
PDBsum1h6d
PubMed11705375
UniProtQ07982|GFO_ZYMMO Glucose--fructose oxidoreductase (Gene Name=gfo)

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