This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1uf8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (23:52, 27 December 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-Phenylalanine==
==Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-Phenylalanine==
-
<StructureSection load='1uf8' size='340' side='right' caption='[[1uf8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+
<StructureSection load='1uf8' size='340' side='right'caption='[[1uf8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1uf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrsp Agrsp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UF8 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1uf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_sp. Agrobacterium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UF8 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ING:D-[(AMINO)CARBONYL]PHENYLALANINE'>ING</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1erz|1erz]], [[1uf4|1uf4]], [[1uf5|1uf5]], [[1uf7|1uf7]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ING:D-[(AMINO)CARBONYL]PHENYLALANINE'>ING</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-carbamoyl-D-amino-acid_hydrolase N-carbamoyl-D-amino-acid hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.77 3.5.1.77] </span></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=1uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uf8 OCA], [https://pdbe.org/1uf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uf8 RCSB], [https://www.ebi.ac.uk/pdbsum/1uf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uf8 ProSAT]</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=1uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uf8 OCA], [http://pdbe.org/1uf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uf8 RCSB], [http://www.ebi.ac.uk/pdbsum/1uf8 PDBsum]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/DCAS_AGRSK DCAS_AGRSK]] The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding which are useful intermediates in the preparation of beta-lactam antibiotics. Industrial production of beta-lactam antibiotics is now being developed using this enzyme.
+
[https://www.uniprot.org/uniprot/DCAS_AGRSK DCAS_AGRSK] The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding which are useful intermediates in the preparation of beta-lactam antibiotics. Industrial production of beta-lactam antibiotics is now being developed using this enzyme.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
-
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uf/1uf8_consurf.spt"</scriptWhenChecked>
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uf/1uf8_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
-
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uf8 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Agrsp]]
+
[[Category: Agrobacterium sp]]
-
[[Category: N-carbamoyl-D-amino-acid hydrolase]]
+
[[Category: Large Structures]]
-
[[Category: Aoki, M]]
+
[[Category: Aoki M]]
-
[[Category: Hashimoto, H]]
+
[[Category: Hashimoto H]]
-
[[Category: Ikenaka, Y]]
+
[[Category: Ikenaka Y]]
-
[[Category: Morikawa, H]]
+
[[Category: Morikawa H]]
-
[[Category: Nakai, T]]
+
[[Category: Nakai T]]
-
[[Category: Sato, M]]
+
[[Category: Sato M]]
-
[[Category: Shimizu, T]]
+
[[Category: Shimizu T]]
-
[[Category: Takahashi, S]]
+
[[Category: Takahashi S]]
-
[[Category: D-amino acid]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: N-carbamyl-d-amino acid amidohydrolase]]
+
-
[[Category: N-carbamyl-d-phenylalanine]]
+

Current revision

Crystal structure of C171A/V236A Mutant of N-carbamyl-D-amino acid amidohydrolase complexed with N-carbamyl-D-Phenylalanine

PDB ID 1uf8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools