1gyn
From Proteopedia
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|PDB= 1gyn |SIZE=350|CAPTION= <scene name='initialview01'>1gyn</scene>, resolution 2.00Å | |PDB= 1gyn |SIZE=350|CAPTION= <scene name='initialview01'>1gyn</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyn OCA], [http://www.ebi.ac.uk/pdbsum/1gyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gyn RCSB]</span> | ||
}} | }} | ||
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[[Category: Kemp, L E.]] | [[Category: Kemp, L E.]] | ||
[[Category: Leonard, G A.]] | [[Category: Leonard, G A.]] | ||
| - | [[Category: CD]] | ||
[[Category: aldolase]] | [[Category: aldolase]] | ||
[[Category: cadmium]] | [[Category: cadmium]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''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 20:54:04 2008'' |
Revision as of 17:54, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Fructose-bisphosphate aldolase, with EC number 4.1.2.13 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE
Overview
Previously determined crystal structures of the zinc enzyme Escherichia coli class II fructose-1,6-bisphosphate aldolase display good agreement for the protein structure but a differing metal-ion organization in the active site. The structure of the enzyme with Cd(2+) in place of Zn(2+) has now been determined to 2.0 A resolution to facilitate cation identification. The protein structure was essentially identical to other structures and five Cd(2+) positions were identified. Two of the cations are at the active site; one corresponds to the catalytic ion and the other provides a structural contribution. These Cd(2+) sites are equivalent to two Zn(2+) ions observed when the enzyme is complexed with a transition-state mimic and confirm our assignment of the roles played by these ions.
About this Structure
1GYN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase., Hall DR, Kemp LE, Leonard GA, Marshall K, Berry A, Hunter WN, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):611-4. Epub 2003, Feb 21. PMID:12595741
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