Structure of PDB 1rye Chain D

Receptor sequence
>1ryeD (length=370) Species: 542 (Zymomonas mobilis) [Search protein sequence]
ATLPAGASQVPTTPAGRPMPYAIRRFGYAIVGLGKYALNQILPGFAGCQH
SRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKIDAVYIIL
PNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAANKKLMIGY
RCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQWRLRRELA
GGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEVEDRIIWQ
MRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQNLISVQTP
GHANQSMMPANNQFSAQLDHLAEAVINNKPVRSPGEEGMQDVRLIQAIYE
AARTGRPVNTDWGYVRQGGY
3D structure
PDB1rye Crystal Structure of the Shifted Form of the Glucose-Fructose Oxidoreductase from Zymomonas mobilis
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K129 Y217
Catalytic site (residue number reindexed from 1) K123 Y211
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 P11 P14 A15 G16 R17 P11 P14 A15 G16 R17
BS02 NDP D L39 G40 K41 Y42 S64 G65 Y87 I105 L106 P107 N108 H111 E128 K129 R157 W199 R200 Y217 L33 G34 K35 Y36 S58 G59 Y81 I99 L100 P101 N102 H105 E122 K123 R151 W193 R194 Y211
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0047061 glucose-fructose oxidoreductase activity
Biological Process
GO:0006061 sorbitol biosynthetic process
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1rye, PDBe:1rye, PDBj:1rye
PDBsum1rye
PubMed
UniProtQ07982|GFO_ZYMMO Glucose--fructose oxidoreductase (Gene Name=gfo)

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