3f80

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==(S)-2-amino-6-nitrohexanoic acid binds to human arginase I through multiple nitro-metal coordination interactions in the binuclear manganese cluster. Resolution 1.60 A.==
==(S)-2-amino-6-nitrohexanoic acid binds to human arginase I through multiple nitro-metal coordination interactions in the binuclear manganese cluster. Resolution 1.60 A.==
-
<StructureSection load='3f80' size='340' side='right' caption='[[3f80]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+
<StructureSection load='3f80' size='340' side='right'caption='[[3f80]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3f80]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F80 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F80 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3f80]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F80 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6HN:6-NITRO-L-NORLEUCINE'>6HN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6HN:6-NITRO-L-NORLEUCINE'>6HN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span></td></tr>
+
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Arginase Arginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </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=3f80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f80 OCA], [http://pdbe.org/3f80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f80 RCSB], [http://www.ebi.ac.uk/pdbsum/3f80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f80 ProSAT]</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=3f80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f80 OCA], [https://pdbe.org/3f80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f80 RCSB], [https://www.ebi.ac.uk/pdbsum/3f80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f80 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
-
[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
+
[[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[https://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 32: Line 32:
==See Also==
==See Also==
-
*[[Arginase|Arginase]]
+
*[[Arginase 3D structures|Arginase 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 39: Line 39:
[[Category: Arginase]]
[[Category: Arginase]]
[[Category: Human]]
[[Category: Human]]
 +
[[Category: Large Structures]]
[[Category: Christianson, D W]]
[[Category: Christianson, D W]]
[[Category: Costanzo, L Di]]
[[Category: Costanzo, L Di]]

Revision as of 09:26, 23 February 2022

(S)-2-amino-6-nitrohexanoic acid binds to human arginase I through multiple nitro-metal coordination interactions in the binuclear manganese cluster. Resolution 1.60 A.

PDB ID 3f80

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools