Protein Overview: gi|160285643, gi...

General Information:
Name(s) found:	gi\|209870414 [NCBI NR] gi\|209870413 [NCBI NR] gi\|209870412 [NCBI NR] gi\|209870411 [NCBI NR] gi\|209870410 [NCBI NR] gi\|209870409 [NCBI NR] gi\|1888485 [NCBI NR] gi\|168177313 [NCBI NR] gi\|168177312 [NCBI NR] gi\|168177311 [NCBI NR] gi\|168177310 [NCBI NR] gi\|160285643 [NCBI NR] gi\|160285642 [NCBI NR] gi\|158428825 [NCBI NR] gi\|158428824 [NCBI NR] gi\|158428823 [NCBI NR] gi\|158428822 [NCBI NR] gi\|118137402 [NCBI NR] gi\|118137401 [NCBI NR]
Description(s) found: Found 22 descriptions. SHOW ALL	gi\|209870414\|pdb\|3BXX\|F Chain F, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|209870413\|pdb\|3BXX\|E Chain E, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|209870412\|pdb\|3BXX\|D Chain D, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|209870411\|pdb\|3BXX\|C Chain C, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|209870410\|pdb\|3BXX\|B Chain B, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|209870409\|pdb\|3BXX\|A Chain A, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|1888485\|emb\|CAA72420.1\| dihydroflavonol 4-reductase [Vitis vinifera] [NCBI NR] gi\|168177313\|pdb\|3C1T\|D Chain D, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|168177312\|pdb\|3C1T\|C Chain C, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|168177311\|pdb\|3C1T\|B Chain B, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|168177310\|pdb\|3C1T\|A Chain A, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol 4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|160285643\|pdb\|2NNL\|F Chain F, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol-4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|160285642\|pdb\|2NNL\|D Chain D, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol-4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|158428825\|pdb\|2IOD\|D Chain D, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol-4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|158428824\|pdb\|2IOD\|C Chain C, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol-4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|158428823\|pdb\|2IOD\|B Chain B, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol-4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|158428822\|pdb\|2IOD\|A Chain A, Binding Of Two Substrate Analogue Molecules To Dihydroflavonol-4-Reductase Alters The Functional Geometry Of The Catalytic Site [NCBI NR] gi\|118137402\|pdb\|2C29\|F Chain F, Structure Of Dihydroflavonol Reductase From Vitis Vinifera At 1.8 A. [NCBI NR] gi\|118137401\|pdb\|2C29\|D Chain D, Structure Of Dihydroflavonol Reductase From Vitis Vinifera At 1.8 A. [NCBI NR]
Organism:	Vitis vinifera
Length:	337 amino acids
Gene Ontology:
Cellular Component:	NONE FOUND
Biological Process:	NONE FOUND
Molecular Function:	NONE FOUND

Sequence:

Sequence:
[PDR BLAST]
[ProtParam]

      1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MGSQSETVCV TGASGFIGSW LVMRLLERGY TVRATVRDPT NVKKVKHLLD LPKAETHLTL  60
   61 WKADLADEGS FDEAIKGCTG VFHVATPMDF ESKDPENEVI KPTIEGMLGI MKSCAAAKTV 120
  121 RRLVFTSSAG TVNIQEHQLP VYDESCWSDM EFCRAKKMTA WMYFVSKTLA EQAAWKYAKE 180
  181 NNIDFITIIP TLVVGPFIMS SMPPSLITAL SPITGNEAHY SIIRQGQFVH LDDLCNAHIY 240
  241 LFENPKAEGR YICSSHDCII LDLAKMLREK YPEYNIPTEF KGVDENLKSV CFSSKKLTDL 300
  301 GFEFKYSLED MFTGAVDTCR AKGLLPPSHE KPVDGKT

Protein Complex Data

No complex found for this protein.

Mass Spectrometry Data

No mass spectrometry results found for this protein.

Yeast Two-Hybrid Data

The following interactions contain this protein:

NOT SHOWING SINGLE HITS. [ Show Single Hits ]

[View our yeast two-hybrid interpretation guidelines.]

No yeast two-hybrid interactions found for this protein.

Protein predicted to be:	GLOBULAR (No transmembrane regions or signal peptide)
Confidence of classification:	0.57

Protein Overview: gi|160285643, gi...

Protein Complex Data

Mass Spectrometry Data

Yeast Two-Hybrid Data

Microscopy / Localization Data

Protein Structure Data

Philius Transmembrane Prediction: