1ne7
From Proteopedia
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|PDB= 1ne7 |SIZE=350|CAPTION= <scene name='initialview01'>1ne7</scene>, resolution 1.75Å | |PDB= 1ne7 |SIZE=350|CAPTION= <scene name='initialview01'>1ne7</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=16G:N-ACETYL-D-GLUCOSAMINE-6-PHOSPHATE'>16G</scene>, <scene name='pdbligand=AGP:2-DEOXY-2-AMINO+GLUCITOL-6-PHOSPHATE'>AGP</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucosamine-6-phosphate_deaminase Glucosamine-6-phosphate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.6 3.5.99.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucosamine-6-phosphate_deaminase Glucosamine-6-phosphate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.6 3.5.99.6] </span> |
|GENE= GNPI OR HLN OR KIAA0060 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= GNPI OR HLN OR KIAA0060 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dea|1DEA]], [[1hot|1HOT]], [[1hor|1HOR]], [[1fs5|1FS5]], [[1fsf|1FSF]], [[1fs6|1FS6]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ne7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ne7 OCA], [http://www.ebi.ac.uk/pdbsum/1ne7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ne7 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an allosteric enzyme that catalyzes the reversible conversion of D-glucosamine-6-phosphate into D-fructose-6-phosphate and ammonium. Here we describe the existence of two mammalian glucosamine-6-phosphate deaminase enzymes. We present the crystallographic structure of one of them, the long human glucosamine-6-phosphate deaminase, at 1.75 A resolution. Crystals belong to the space group P2(1)2(1)2(1) and present a whole hexamer in the asymmetric unit. The active-site lid (residues 162-182) presented significant structural differences among monomers. Interestingly the region with the largest differences, when compared with the Escherichia coli homologue, was found to be close to the active site. These structural differences can be related to the kinetic and allosteric properties of both mammalian enzymes. | Glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an allosteric enzyme that catalyzes the reversible conversion of D-glucosamine-6-phosphate into D-fructose-6-phosphate and ammonium. Here we describe the existence of two mammalian glucosamine-6-phosphate deaminase enzymes. We present the crystallographic structure of one of them, the long human glucosamine-6-phosphate deaminase, at 1.75 A resolution. Crystals belong to the space group P2(1)2(1)2(1) and present a whole hexamer in the asymmetric unit. The active-site lid (residues 162-182) presented significant structural differences among monomers. Interestingly the region with the largest differences, when compared with the Escherichia coli homologue, was found to be close to the active site. These structural differences can be related to the kinetic and allosteric properties of both mammalian enzymes. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Huntington disease-like 3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604802 604802]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Morante, M L.]] | [[Category: Morante, M L.]] | ||
[[Category: Valderrama, B.]] | [[Category: Valderrama, B.]] | ||
| - | [[Category: 16G]] | ||
| - | [[Category: AGP]] | ||
| - | [[Category: GLC]] | ||
| - | [[Category: SO4]] | ||
[[Category: conformational difference]] | [[Category: conformational difference]] | ||
[[Category: conformational disorder]] | [[Category: conformational disorder]] | ||
[[Category: v-type like allosteric enzyme]] | [[Category: v-type like allosteric 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 22:29:10 2008'' |
Revision as of 19:29, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | GNPI OR HLN OR KIAA0060 (Homo sapiens) | ||||||
| Activity: | Glucosamine-6-phosphate deaminase, with EC number 3.5.99.6 | ||||||
| Related: | 1DEA, 1HOT, 1HOR, 1FS5, 1FSF, 1FS6
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN GLUCOSAMINE-6-PHOSPHATE DEAMINASE ISOMERASE AT 1.75 A RESOLUTION COMPLEXED WITH N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AND 2-DEOXY-2-AMINO-GLUCITOL-6-PHOSPHATE
Overview
Glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an allosteric enzyme that catalyzes the reversible conversion of D-glucosamine-6-phosphate into D-fructose-6-phosphate and ammonium. Here we describe the existence of two mammalian glucosamine-6-phosphate deaminase enzymes. We present the crystallographic structure of one of them, the long human glucosamine-6-phosphate deaminase, at 1.75 A resolution. Crystals belong to the space group P2(1)2(1)2(1) and present a whole hexamer in the asymmetric unit. The active-site lid (residues 162-182) presented significant structural differences among monomers. Interestingly the region with the largest differences, when compared with the Escherichia coli homologue, was found to be close to the active site. These structural differences can be related to the kinetic and allosteric properties of both mammalian enzymes.
About this Structure
1NE7 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1D9T. Full crystallographic information is available from OCA.
Reference
Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study., Arreola R, Valderrama B, Morante ML, Horjales E, FEBS Lett. 2003 Sep 11;551(1-3):63-70. PMID:12965206
Page seeded by OCA on Sun Mar 30 22:29:10 2008
