1h3m: Difference between revisions
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|PDB= 1h3m |SIZE=350|CAPTION= <scene name='initialview01'>1h3m</scene>, resolution 2.40Å | |PDB= 1h3m |SIZE=350|CAPTION= <scene name='initialview01'>1h3m</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=AC1:N2p+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:N2p+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=N2P:PENTANE-1,5-DIAMINE'>N2P</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/2-C-methyl-D-erythritol_4-phosphate_cytidylyltransferase 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.60 2.7.7.60] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/2-C-methyl-D-erythritol_4-phosphate_cytidylyltransferase 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.60 2.7.7.60] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3m OCA], [http://www.ebi.ac.uk/pdbsum/1h3m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h3m RCSB]</span> | |||
}} | }} | ||
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[[Category: Hunter, W N.]] | [[Category: Hunter, W N.]] | ||
[[Category: Kemp, L E.]] | [[Category: Kemp, L E.]] | ||
[[Category: isoprenoid]] | [[Category: isoprenoid]] | ||
[[Category: synthetase]] | [[Category: synthetase]] | ||
''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 20:56:59 2008'' | ||
Revision as of 17:57, 30 March 2008
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| 1h3m, resolution 2.40Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | AC1 | ||||||||||||
| Ligands: | CL, N2P | ||||||||||||
| Activity: | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, with EC number 2.7.7.60 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2C-METHYL-D-ERYTHRITOL SYNTHETASE
Overview
2-C-Methyl-D-erythritol 4-phosphate cytidylyltransferase is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. The structure of a tetragonal crystal form has been solved by molecular replacement and refined to 2.4 A resolution. Structure and sequence comparisons suggest that the enzyme is a suitable target for a structure-based approach to the development of novel broad-spectrum antibiotics. However, the absence of ligands in the enzyme active site together with the moderate resolution of the structure indicates that this tetragonal crystal form is inferior to that of a previously reported highly ordered monoclinic form [Richard et al. (2001), Nature Struct. Biol. 8, 641-647].
About this Structure
1H3M is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase., Kemp LE, Bond CS, Hunter WN, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):607-10. Epub 2003, Feb 21. PMID:12595740
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