Structure of PDB 1h6d Chain D

Receptor sequence
>1h6dD (length=382) Species: 542 (Zymomonas mobilis) [Search protein sequence]
AATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILP
GFAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKI
DAVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAAN
KKLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQW
RLRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEV
EDRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQN
LISVQTPGHANQSMMPQFIMPANNQFSAQLDHLAEAVINNKPVRSPGEEG
MQDVRLIQAIYEAARTGRPVNTDWGYVRQGGY
3D structure
PDB1h6d Crystal Structures of the Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas Mobilis and its Complexes with Bound Ligands
ChainD
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) 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 D A67 G68 R69 A16 G17 R18
BS02 NDP D G90 L91 G92 K93 Y94 S116 G117 K121 Y139 I157 L158 P159 N160 H163 E180 K181 R209 A248 W251 R252 Y269 G39 L40 G41 K42 Y43 S65 G66 K70 Y88 I106 L107 P108 N109 H112 E129 K130 R158 A197 W200 R201 Y218
BS03 GOL D R252 D265 R201 D214
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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