1N5U

X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH HEME

Summary for 1N5U

• Entry DOI: 10.2210/pdb1n5u/pdb
• Descriptor: SERUM ALBUMIN, MYRISTIC ACID, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: plasma protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02768
• Total number of polymer chains: 1
• Total formula weight: 68329.56

Authors

Wardell, M.,Wang, Z.,Ho, J.X.,Robert, J.,Ruker, F.,Ruble, J.,Carter, D.C. (deposition date: 2002-11-07, release date: 2003-06-24, Last modification date: 2011-07-13)

Primary citation

Wardell, M.,Wang, Z.,Ho, J.X.,Robert, J.,Ruker, F.,Ruble, J.,Carter, D.C.
The Atomic Structure of Human Methemalbumin at 1.9 A
Biochem.Biophys.Res.Commun., 291:813-819, 2002

PubMed Abstract: 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.

PubMed: 11866438
DOI: 10.1006/bbrc.2002.6540

Experimental method

X-RAY DIFFRACTION (1.9 Å)