1b7z
From Proteopedia
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- | [[Image:1b7z.jpg|left|200px]] | + | [[Image:1b7z.jpg|left|200px]] |
- | + | ||
- | '''STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM''' | + | {{Structure |
+ | |PDB= 1b7z |SIZE=350|CAPTION= <scene name='initialview01'>1b7z</scene>, resolution 2.7Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=OXL:OXALATE ION'>OXL</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1B7Z is a [ | + | 1B7Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B7Z OCA]. |
==Reference== | ==Reference== | ||
- | Structure of oxalate-substituted diferric mare lactoferrin at 2.7 A resolution., Sharma AK, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1792-8. PMID:[http:// | + | Structure of oxalate-substituted diferric mare lactoferrin at 2.7 A resolution., Sharma AK, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1792-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10531474 10531474] |
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metal binding site]] | [[Category: metal binding site]] | ||
- | ''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 10:07:32 2008'' |
Revision as of 08:07, 20 March 2008
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, resolution 2.7Å | |||||||
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Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM
Overview
Lactoferrin binds two Fe(3+) and two CO(2-)(3) ions with high affinity. It can also bind other metal ions and anions. In order to determine the perturbations in the environments of the binding sites in the N and C lobes and elsewhere in the protein, the crystal structure of oxalate-substituted diferric mare lactoferrin has been determined at 2.7 A resolution. The final model has a crystallographic R factor of 21.3% for all data in the resolution range 17.0-2.7 A. The substitution of an oxalate anion does not perturb the overall structure of the protein, but produces several significant changes at the metal-binding and anion-binding sites. The binding of the oxalate anion is symmetrical in both the N and C lobes, unlike in diferric dioxalate human lactoferrin, where the oxalate anion binds the metal ion symmetrically in the C lobe and asymmetrically in the N lobe.
About this Structure
1B7Z is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
Structure of oxalate-substituted diferric mare lactoferrin at 2.7 A resolution., Sharma AK, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1792-8. PMID:10531474
Page seeded by OCA on Thu Mar 20 10:07:32 2008
Categories: Equus caballus | Single protein | Sharma, A K. | Singh, T P. | FE | OXL | Dioxalate | Lactoferrin | Metal binding site