Structure of PDB 2glx Chain D

Receptor sequence
>2glxD (length=332) Species: 106592 (Ensifer adhaerens) [Search protein sequence]
NRWGLIGASTIAREWVIGAIRATGGEVVSMMSTSAERGAAYATENGIGKS
VTSVEELVGDPDVDAVYVSTTNELHREQTLAAIRAGKHVLCEKPLAMTLE
DAREMVVAAREAGVVLGTNHHLRNAAAHRAMRDAIAEGRIGRPIAARVFH
AVYLPPHLQGWRLERPEAGGGVILDITVHDADTLRFVLNDDPAEAVAISH
SAGMGKEGVEDGVMGVLRFQSGVIAQFHDAFTTKFAETGFEVHGTEGSLI
GRNVMTQKPVGTVTLRNAEGESQLPLDPANLYETALAAFHSAIEGHGQPS
ATGEDGVWSLATGLAVVKAAATGQAAEIETGL
3D structure
PDB2glx Crystal Structure of NADP(H)-Dependent 1,5-Anhydro-d-fructose Reductase from Sinorhizobium morelense at 2.2 A Resolution: Construction of a NADH-Accepting Mutant and Its Application in Rare Sugar Synthesis
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K94 H180
Catalytic site (residue number reindexed from 1) K93 H179
Enzyme Commision number 1.1.1.292: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming).
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 ACT D K94 H180 K93 H179
BS02 NDP D G8 A9 S10 T11 I12 S33 T34 R38 S70 T71 N73 H76 E93 K94 N120 W162 R163 Q258 Y283 G7 A8 S9 T10 I11 S32 T33 R37 S69 T70 N72 H75 E92 K93 N119 W161 R162 Q257 Y282
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0033712 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity

View graph for
Molecular Function
External links
PDB RCSB:2glx, PDBe:2glx, PDBj:2glx
PDBsum2glx
PubMed16906761
UniProtQ2I8V6|AFR_ENSAD 1,5-anhydro-D-fructose reductase (Gene Name=afr)

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