2vi8: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vi8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VI8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VI8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2vi8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VI8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VI8 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vgu|2vgu]], [[1yjy|1yjy]], [[1yjs|1yjs]], [[1kl2|1kl2]], [[1kl1|1kl1]], [[1kkp|1kkp]], [[2vgs|2vgs]], [[1yjz|1yjz]], [[2vgt|2vgt]], [[2vgv|2vgv]], [[1kkj|1kkj]], [[2vgw|2vgw]], [[2vib|2vib]], [[2via|2via]], [[2vi9|2vi9]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vgu|2vgu]], [[1yjy|1yjy]], [[1yjs|1yjs]], [[1kl2|1kl2]], [[1kl1|1kl1]], [[1kkp|1kkp]], [[2vgs|2vgs]], [[1yjz|1yjz]], [[2vgt|2vgt]], [[2vgv|2vgv]], [[1kkj|1kkj]], [[2vgw|2vgw]], [[2vib|2vib]], [[2via|2via]], [[2vi9|2vi9]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vi8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vi8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vi8 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vi8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vi8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vi8 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/Q7SIB6_BACST Q7SIB6_BACST]] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity).[HAMAP-Rule:MF_00051] Interconversion of serine and glycine (By similarity).[RuleBase:RU000585] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: Glycine hydroxymethyltransferase]] | [[Category: Glycine hydroxymethyltransferase]] | ||
[[Category: Bhavani, B S | [[Category: Bhavani, B S]] | ||
[[Category: Murthy, M R.N | [[Category: Murthy, M R.N]] | ||
[[Category: Prakash, V | [[Category: Prakash, V]] | ||
[[Category: Rajaram, V | [[Category: Rajaram, V]] | ||
[[Category: Rao, N Appaji | [[Category: Rao, N Appaji]] | ||
[[Category: Savithri, H S | [[Category: Savithri, H S]] | ||
[[Category: E53q]] | [[Category: E53q]] | ||
[[Category: Enzyme memory]] | [[Category: Enzyme memory]] | ||
Revision as of 00:30, 25 December 2014
CRYSTAL STRUCTURE OF S172ABSSHMT INTERNAL ALDIMINECRYSTAL STRUCTURE OF S172ABSSHMT INTERNAL ALDIMINE
Structural highlights
Function[Q7SIB6_BACST] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity).[HAMAP-Rule:MF_00051] Interconversion of serine and glycine (By similarity).[RuleBase:RU000585] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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