2hmq
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2hmq.gif|left|200px]] | + | [[Image:2hmq.gif|left|200px]] |
| - | + | ||
| - | '''THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 2hmq |SIZE=350|CAPTION= <scene name='initialview01'>2hmq</scene>, resolution 1.66Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2HMQ is a [ | + | 2HMQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Themiste_dyscritum Themiste dyscritum]. This structure supersedes the now removed PDB entries 1HMQ, 1HMM and 1HMN. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMQ OCA]. |
==Reference== | ==Reference== | ||
| - | Structures of met and azidomet hemerythrin at 1.66 A resolution., Holmes MA, Stenkamp RE, J Mol Biol. 1991 Aug 5;220(3):723-37. PMID:[http:// | + | Structures of met and azidomet hemerythrin at 1.66 A resolution., Holmes MA, Stenkamp RE, J Mol Biol. 1991 Aug 5;220(3):723-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1870128 1870128] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Themiste dyscritum]] | [[Category: Themiste dyscritum]] | ||
| Line 19: | Line 28: | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''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 17:18:54 2008'' |
Revision as of 15:18, 20 March 2008
| |||||||
| , resolution 1.66Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION
Overview
The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact.
About this Structure
2HMQ is a Single protein structure of sequence from Themiste dyscritum. This structure supersedes the now removed PDB entries 1HMQ, 1HMM and 1HMN. Full crystallographic information is available from OCA.
Reference
Structures of met and azidomet hemerythrin at 1.66 A resolution., Holmes MA, Stenkamp RE, J Mol Biol. 1991 Aug 5;220(3):723-37. PMID:1870128
Page seeded by OCA on Thu Mar 20 17:18:54 2008
