1ouu
From Proteopedia
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|PDB= 1ouu |SIZE=350|CAPTION= <scene name='initialview01'>1ouu</scene>, resolution 2.5Å | |PDB= 1ouu |SIZE=350|CAPTION= <scene name='initialview01'>1ouu</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ouu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ouu OCA], [http://www.ebi.ac.uk/pdbsum/1ouu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ouu RCSB]</span> | ||
}} | }} | ||
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[[Category: Tame, J.]] | [[Category: Tame, J.]] | ||
[[Category: Wilson, J.]] | [[Category: Wilson, J.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: CMO]] | ||
| - | [[Category: HEM]] | ||
[[Category: erythrocyte]] | [[Category: erythrocyte]] | ||
[[Category: heme]] | [[Category: heme]] | ||
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[[Category: respiratory protein]] | [[Category: respiratory 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 22:50:39 2008'' |
Revision as of 19:50, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CARBONMONOXY TROUT HEMOGLOBIN I
Overview
We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 angstroms and 2.5 angstroms, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions.
About this Structure
1OUU is a Protein complex structure of sequences from Oncorhynchus mykiss. Full crystallographic information is available from OCA.
Reference
The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms., Tame JR, Wilson JC, Weber RE, J Mol Biol. 1996 Jun 21;259(4):749-60. PMID:8683580
Page seeded by OCA on Sun Mar 30 22:50:39 2008
