1b7z
From Proteopedia
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|PDB= 1b7z |SIZE=350|CAPTION= <scene name='initialview01'>1b7z</scene>, resolution 2.7Å | |PDB= 1b7z |SIZE=350|CAPTION= <scene name='initialview01'>1b7z</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> | + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b7z OCA], [http://www.ebi.ac.uk/pdbsum/1b7z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b7z RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Sharma, A K.]] | [[Category: Sharma, A K.]] | ||
[[Category: Singh, T P.]] | [[Category: Singh, T P.]] | ||
| - | [[Category: FE]] | ||
| - | [[Category: OXL]] | ||
[[Category: dioxalate]] | [[Category: dioxalate]] | ||
[[Category: lactoferrin]] | [[Category: lactoferrin]] | ||
[[Category: metal binding site]] | [[Category: metal binding site]] | ||
| - | ''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 18:55:30 2008'' |
Revision as of 15:55, 30 March 2008
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| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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