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1ndh

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[[Image:1ndh.jpg|left|200px]]<br /><applet load="1ndh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ndh.jpg|left|200px]]
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caption="1ndh, resolution 2.1&Aring;" />
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'''CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION'''<br />
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{{Structure
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|PDB= 1ndh |SIZE=350|CAPTION= <scene name='initialview01'>1ndh</scene>, resolution 2.1&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cytochrome-b5_reductase Cytochrome-b5 reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.2 1.6.2.2]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NDH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-b5_reductase Cytochrome-b5 reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.2 1.6.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NDH OCA].
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1NDH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NDH OCA].
==Reference==
==Reference==
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Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution., Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K, Miki K, Biochemistry. 1995 Mar 7;34(9):2763-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7893687 7893687]
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Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution., Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K, Miki K, Biochemistry. 1995 Mar 7;34(9):2763-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7893687 7893687]
[[Category: Cytochrome-b5 reductase]]
[[Category: Cytochrome-b5 reductase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: electron transport (flavo protein)]]
[[Category: electron transport (flavo protein)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:55:27 2008''

Revision as of 10:55, 20 March 2008

Image:1ndh.jpg


PDB ID 1ndh

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands:
Activity: Cytochrome-b5 reductase, with EC number 1.6.2.2
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION


Overview

The three-dimensional structure of NADH-cytochrome b5 reductase from pig liver microsomes has been determined at 2.4 A resolution by X-ray crystallography. The molecular structure reveals two domains, the FAD binding domain and the NADH domain. A large cleft lies between these two domains and contains the binding site for the FAD prosthetic group. The backbone structure of the FAD binding domain has a great similarity to that of ferredoxin-NADP+ reductase [Karplus, P. A., Daniels, M. J., & Herriott, J. R. (1991) Science 251, 60-65], in spite of the relatively low sequence homology (about 15%) between the two enzymes. On the other hand, the structure of the NADH domain has several structural differences from that of the NADP+ domain of ferredoxin-NADP+ reductase. The size of the cleft between the two domains is larger in NADH-cytochrome b5 reductase than in ferredoxin-NADP+ reductase, which may be responsible for the observed difference in the nucleotide accessibility in the two enzymes.

About this Structure

1NDH is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution., Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K, Miki K, Biochemistry. 1995 Mar 7;34(9):2763-7. PMID:7893687

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