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1umk
From Proteopedia
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|PDB= 1umk |SIZE=350|CAPTION= <scene name='initialview01'>1umk</scene>, resolution 1.75Å | |PDB= 1umk |SIZE=350|CAPTION= <scene name='initialview01'>1umk</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1umk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umk OCA], [http://www.ebi.ac.uk/pdbsum/1umk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1umk RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Takeshita, M.]] | [[Category: Takeshita, M.]] | ||
[[Category: Yubisui, T.]] | [[Category: Yubisui, T.]] | ||
| - | [[Category: FAD]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: fad-binding domain]] | [[Category: fad-binding domain]] | ||
| Line 36: | Line 38: | ||
[[Category: nadh-binding domain]] | [[Category: nadh-binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:12:19 2008'' |
Revision as of 21:12, 30 March 2008
| |||||||
| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Cytochrome-b5 reductase, with EC number 1.6.2.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase
Overview
Erythrocyte NADH-cytochrome b(5) reductase reduces methaemoglobin to functional haemoglobin. In order to examine the function of the enzyme, the structure of NADH-cytochrome b(5) reductase from human erythrocytes has been determined and refined by X-ray crystallography. At 1.75 A resolution, the root-mean-square deviations (r.m.s.d.) from standard bond lengths and angles are 0.006 A and 1.03 degrees , respectively. The molecular structure was compared with those of rat NADH-cytochrome b(5) reductase and corn nitrate reductase. The human reductase resembles the rat reductase in overall structure as well as in many side chains. Nevertheless, there is a large main-chain shift from the human reductase to the rat reductase or the corn reductase caused by a single-residue replacement from proline to threonine. A model of the complex between cytochrome b(5) and the human reductase has been built and compared with that of the haem-containing domain of the nitrate reductase molecule. The interaction between cytochrome b(5) and the human reductase differs from that of the nitrate reductase because of differences in the amino-acid sequences. The structures around 15 mutation sites of the human reductase have been examined for the influence of residue substitutions using the program ROTAMER. Five mutations in the FAD-binding domain seem to be related to cytochrome b(5).
About this Structure
1UMK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human erythrocyte NADH-cytochrome b5 reductase., Bando S, Takano T, Yubisui T, Shirabe K, Takeshita M, Nakagawa A, Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):1929-34. Epub 2004, Oct 20. PMID:15502298
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