1DWR
MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH CO
Summary for 1DWR
| Entry DOI | 10.2210/pdb1dwr/pdb |
| Related | 1AZI 1BJE 1DWS 1DWT 1HRM 1HSY 1RSE 1WLA 1XCH 1YMA 1YMB 1YMC |
| Descriptor | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (5 entities in total) |
| Functional Keywords | oxygen transport, respiratory protein |
| Biological source | Equus caballus (Horse) |
| Total number of polymer chains | 1 |
| Total formula weight | 17820.14 |
| Authors | Chu, K.,Vojtechovsky, J.,McMahon, B.H.,Sweet, R.M.,Berendzen, J.,Schlichting, I. (deposition date: 1999-12-11, release date: 2000-03-03, Last modification date: 2023-12-06) |
| Primary citation | Chu, K.,Vojtechovsky, J.,Mcmahon, B.H.,Sweet, R.M.,Berendzen, J.,Schlichting, I. Crystal Structure of a New Ligand Binding Intermediate in Wildtype Carbonmonoxy Myoglobin Nature, 403:921-, 2000 Cited by PubMed Abstract: Small molecules such as NO, O2, CO or H2 are important biological ligands that bind to metalloproteins to function crucially in processes such as signal transduction, respiration and catalysis. A key issue for understanding the regulation of reaction mechanisms in these systems is whether ligands gain access to the binding sites through specific channels and docking sites, or by random diffusion through the protein matrix. A model system for studying this issue is myoglobin, a simple haem protein. Myoglobin has been studied extensively by spectroscopy, crystallography, computation and theory. It serves as an aid to oxygen diffusion but also binds carbon monoxide, a byproduct of endogenous haem catabolism. Molecular dynamics simulations, random mutagenesis and flash photolysis studies indicate that ligand migration occurs through a limited number of pathways involving docking sites. Here we report the 1.4 A resolution crystal structure of a ligand-binding intermediate in carbonmonoxy myoglobin that may have far-reaching implications for understanding the dynamics of ligand binding and catalysis. PubMed: 10706294DOI: 10.1038/35002641 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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