1hrk
From Proteopedia
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| - | [[Image:1hrk.gif|left|200px]] | + | [[Image:1hrk.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE''' | + | {{Structure |
| + | |PDB= 1hrk |SIZE=350|CAPTION= <scene name='initialview01'>1hrk</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene> and <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HRK is a [ | + | 1HRK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRK OCA]. |
==Reference== | ==Reference== | ||
| - | The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis., Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC, Nat Struct Biol. 2001 Feb;8(2):156-60. PMID:[http:// | + | The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis., Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC, Nat Struct Biol. 2001 Feb;8(2):156-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11175906 11175906] |
[[Category: Ferrochelatase]] | [[Category: Ferrochelatase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: protoheme ferro-lyase]] | [[Category: protoheme ferro-lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:40:42 2008'' |
Revision as of 09:40, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Ferrochelatase, with EC number 4.99.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE
Contents |
Overview
Human ferrochelatase (E.C. 4.99.1.1) is a homodimeric (86 kDa) mitochondrial membrane-associated enzyme that catalyzes the insertion of ferrous iron into protoporphyrin to form heme. We have determined the 2.0 A structure from the single wavelength iron anomalous scattering signal. The enzyme contains two NO-sensitive and uniquely coordinated [2Fe-2S] clusters. Its membrane association is mediated in part by a 12-residue hydrophobic lip that also forms the entrance to the active site pocket. The positioning of highly conserved residues in the active site in conjunction with previous biochemical studies support a catalytic model that may have significance in explaining the enzymatic defects that lead to the human inherited disease erythropoietic protoporphyria.
Disease
Known diseases associated with this structure: Protoporphyria, erythropoietic OMIM:[177000], Protoporphyria, erythropoietic, recessive, with liver failure OMIM:[177000]
About this Structure
1HRK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis., Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC, Nat Struct Biol. 2001 Feb;8(2):156-60. PMID:11175906
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