3tsq
From Proteopedia
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| - | [[Image:3tsq.png|left|200px]] | ||
| - | + | ==Crystal structure of E. coli HypF with ATP and Carbamoyl phosphate== | |
| - | + | <StructureSection load='3tsq' size='340' side='right'caption='[[3tsq]], [[Resolution|resolution]] 2.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3tsq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TSQ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA0:5-O-[(S)-(CARBAMOYLOXY)(HYDROXY)PHOSPHORYL]ADENOSINE'>CA0</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | == | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsq OCA], [https://pdbe.org/3tsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tsq RCSB], [https://www.ebi.ac.uk/pdbsum/3tsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tsq ProSAT]</span></td></tr> |
| - | [[3tsq]] is a 1 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0H3JHT3_ECO57 A0A0H3JHT3_ECO57] Involved in the maturation of [NiFe] hydrogenases. Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase using carbamoylphosphate as a substrate and transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide.[PIRNR:PIRNR006256] | ||
==See Also== | ==See Also== | ||
| - | *[[ | + | *[[HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures|HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Escherichia coli O157:H7]] | |
| - | [[Category: Escherichia coli]] | + | [[Category: Large Structures]] |
| - | [[Category: Cygler | + | [[Category: Cygler M]] |
| - | [[Category: Li | + | [[Category: Li Y]] |
| - | [[Category: Petkun | + | [[Category: Petkun S]] |
| - | [[Category: Shi | + | [[Category: Shi R]] |
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Current revision
Crystal structure of E. coli HypF with ATP and Carbamoyl phosphate
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