1n5u
From Proteopedia
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|PDB= 1n5u |SIZE=350|CAPTION= <scene name='initialview01'>1n5u</scene>, resolution 1.90Å | |PDB= 1n5u |SIZE=350|CAPTION= <scene name='initialview01'>1n5u</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n5u OCA], [http://www.ebi.ac.uk/pdbsum/1n5u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n5u RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The high resolution structure of hemalbumin was determined by single crystal X-ray diffraction to a resolution of 1.9 A. The structure revealed the protoporphyrin IX bound to a single site within a hydrophobic cavity in subdomain IB, one of the principal binding sites for long chain fatty acid. The iron is penta coordinated with the fifth ligand comprised of the hydroxyl oxygen of Tyr-161 (phenolic oxygen to heme plane distance: 2.73 A) in an otherwise completely hydrophobic pocket. The heme propionic acid residues form salt bridges with His-142 and Lys-190, which together with a series of hydrophobic interactions, enclose and secure the heme within the IB helical motif. A detailed discussion of the structure together with its implications for the development of potential blood substitutes is presented. | The high resolution structure of hemalbumin was determined by single crystal X-ray diffraction to a resolution of 1.9 A. The structure revealed the protoporphyrin IX bound to a single site within a hydrophobic cavity in subdomain IB, one of the principal binding sites for long chain fatty acid. The iron is penta coordinated with the fifth ligand comprised of the hydroxyl oxygen of Tyr-161 (phenolic oxygen to heme plane distance: 2.73 A) in an otherwise completely hydrophobic pocket. The heme propionic acid residues form salt bridges with His-142 and Lys-190, which together with a series of hydrophobic interactions, enclose and secure the heme within the IB helical motif. A detailed discussion of the structure together with its implications for the development of potential blood substitutes is presented. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Analbuminemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]], Dysalbuminemic hyperthyroxinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]], Dysalbuminemic hyperzincemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103600 103600]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Wang, Z.]] | [[Category: Wang, Z.]] | ||
[[Category: Wardell, M.]] | [[Category: Wardell, M.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: MYR]] | ||
[[Category: plasma protein]] | [[Category: plasma protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:25:50 2008'' |
Revision as of 19:25, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH HEME
Overview
The high resolution structure of hemalbumin was determined by single crystal X-ray diffraction to a resolution of 1.9 A. The structure revealed the protoporphyrin IX bound to a single site within a hydrophobic cavity in subdomain IB, one of the principal binding sites for long chain fatty acid. The iron is penta coordinated with the fifth ligand comprised of the hydroxyl oxygen of Tyr-161 (phenolic oxygen to heme plane distance: 2.73 A) in an otherwise completely hydrophobic pocket. The heme propionic acid residues form salt bridges with His-142 and Lys-190, which together with a series of hydrophobic interactions, enclose and secure the heme within the IB helical motif. A detailed discussion of the structure together with its implications for the development of potential blood substitutes is presented.
About this Structure
1N5U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The atomic structure of human methemalbumin at 1.9 A., Wardell M, Wang Z, Ho JX, Robert J, Ruker F, Ruble J, Carter DC, Biochem Biophys Res Commun. 2002 Mar 8;291(4):813-9. PMID:11866438
Page seeded by OCA on Sun Mar 30 22:25:50 2008
