1fua
From Proteopedia
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|PDB= 1fua |SIZE=350|CAPTION= <scene name='initialview01'>1fua</scene>, resolution 1.92Å | |PDB= 1fua |SIZE=350|CAPTION= <scene name='initialview01'>1fua</scene>, resolution 1.92Å | ||
|SITE= <scene name='pdbsite=ACT:The+Active+Center+Is+Defined+By+The+Zn+Ion+And+The+Four+...'>ACT</scene> and <scene name='pdbsite=PBS:The+Substrate+Phosphate+Binding+Site+Near+The+Active+Cen+...'>PBS</scene> | |SITE= <scene name='pdbsite=ACT:The+Active+Center+Is+Defined+By+The+Zn+Ion+And+The+Four+...'>ACT</scene> and <scene name='pdbsite=PBS:The+Substrate+Phosphate+Binding+Site+Near+The+Active+Cen+...'>PBS</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/L-fuculose-phosphate_aldolase L-fuculose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/L-fuculose-phosphate_aldolase L-fuculose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fua OCA], [http://www.ebi.ac.uk/pdbsum/1fua PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fua RCSB]</span> | ||
}} | }} | ||
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[[Category: Dreyer, M K.]] | [[Category: Dreyer, M K.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: class ii aldolase]] | [[Category: class ii aldolase]] | ||
[[Category: lyase (aldehyde)]] | [[Category: lyase (aldehyde)]] | ||
[[Category: zinc enzyme]] | [[Category: zinc enzyme]] | ||
| - | ''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 20:30:25 2008'' |
Revision as of 17:30, 30 March 2008
| |||||||
| , resolution 1.92Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , , | ||||||
| Activity: | L-fuculose-phosphate aldolase, with EC number 4.1.2.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T
Overview
The structure of the class II zinc-ion dependent L-fuculose-1-phosphate aldolase from Escherichia coli in its tetragonal crystal form has been established at 1.92 A resolution. The homotetrameric enzyme has a molecular mass of 4 x 24 kDa and follows C(4) symmetry. The structure model is exactly symmetrical, which contradicts an observed birefringence anomaly of the crystals. The four catalytic centers are located in deep clefts at the interfaces of adjacent subunits. The zinc ion is coordinated by three histidines and one glutamate in an almost tetrahedral arrangement. In contrast to numerous other catalytically competent zinc ions, there is no water molecule in the ligand sphere. Replacement of zinc by a cobalt ion caused only small structural changes. A search through the Protein Data Bank indicated that the chain fold is novel. Sequence homology searches revealed a significant similarity to the bacterial L-ribulose-5-phosphate 4-epimerase.
About this Structure
1FUA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli., Dreyer MK, Schulz GE, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1082-91. PMID:15299567
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