1jdo: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1jdo |SIZE=350|CAPTION= <scene name='initialview01'>1jdo</scene>, resolution 1.90Å | |PDB= 1jdo |SIZE=350|CAPTION= <scene name='initialview01'>1jdo</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdo OCA], [http://www.ebi.ac.uk/pdbsum/1jdo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jdo RCSB]</span> | |||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Brucker, E A.]] | [[Category: Brucker, E A.]] | ||
[[Category: Jr., G N.Phillips.]] | [[Category: Jr., G N.Phillips.]] | ||
[[Category: globin]] | [[Category: globin]] | ||
[[Category: heme]] | [[Category: heme]] | ||
| Line 33: | Line 33: | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
''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 21:32:10 2008'' | ||
Revision as of 21:32, 30 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)
OverviewOverview
The structure of the ferrous nitric oxide form of native sperm whale myoglobin has been determined by X-ray crystallography to 1.7 angstroms resolution. The nitric oxide ligand is bent with respect to the heme plane: the Fe-N-O angle is 112 degrees. This angle is smaller than those observed in model compounds and in lupin leghemoglobin. The exact angle appears to be influenced by the strength of the proximal bond and hydrogen bonding interactions between the distal histidine and the bound ligand. Specifically, the N(epsilon) atom of histidine64 is located 2.8 angstroms away from the nitrogen atom of the bound ligand, implying electrostatic stabilization of the FeNO complex. This interpretation is supported by mutagenesis studies. When histidine64 is replaced with apolar amino acids, the rate of nitric oxide dissociation from myoglobin increases tenfold.
About this StructureAbout this Structure
1JDO is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
ReferenceReference
Nitric oxide myoglobin: crystal structure and analysis of ligand geometry., Brucker EA, Olson JS, Ikeda-Saito M, Phillips GN Jr, Proteins. 1998 Mar 1;30(4):352-6. PMID:9533619
Page seeded by OCA on Sun Mar 30 21:32:10 2008