Structure of PDB 1evj Chain B

Receptor sequence
>1evjB (length=338) Species: 542 (Zymomonas mobilis) [Search protein sequence]
RRFGYAIVGLGKYALNQILPGFAGCQHSRIEALVDGNAEKAKIVAAEYGV
DPRKIYDYSNFDKIAKDPKIDAVYIILPNSLHAEFAIRAFKAGKHVMCEK
PMATSVADCQRMIDAAKAANKKLMIGYRCHYDPMNRAAVKLIRENQLGKL
GMVTTDNSDVMDQNDPAQQWRLRRELAGGGSLMDIGIYGLNGTRYLLGEE
PIEVRAYTYSDPNDERFVEVEDRIIWQMRFRSGALSHGASSYSTTTTSRF
SVQGDKAVLLMDPATGYYQNLISVQTPANNQFSAQLDHLAEAVINNKPVR
SPGEEGMQDVRLIQAIYEAARTGRPVNTDWGYVRQGGY
3D structure
PDB1evj Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation.
ChainB
Resolution2.7 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) K100 Y188
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 NAD B L39 G40 K41 Y42 I105 L106 P107 N108 H111 E128 K129 R157 W199 R200 Y217 Y296 L10 G11 K12 Y13 I76 L77 P78 N79 H82 E99 K100 R128 W170 R171 Y188 Y267
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:1evj, PDBe:1evj, PDBj:1evj
PDBsum1evj
PubMed11099381
UniProtQ07982|GFO_ZYMMO Glucose--fructose oxidoreductase (Gene Name=gfo)

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