1z83: Difference between revisions

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<StructureSection load='1z83' size='340' side='right'caption='[[1z83]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1z83' size='340' side='right'caption='[[1z83]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1z83]] is a 3 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=1Z83 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z83 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1z83]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z83 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.9&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </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=1z83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z83 OCA], [https://pdbe.org/1z83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z83 RCSB], [https://www.ebi.ac.uk/pdbsum/1z83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z83 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z83 OCA], [http://pdbe.org/1z83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z83 RCSB], [http://www.ebi.ac.uk/pdbsum/1z83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z83 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/KAD1_HUMAN KAD1_HUMAN]] Defects in AK1 are the cause of hemolytic anemia due to adenylate kinase deficiency (HAAKD) [MIM:[http://omim.org/entry/612631 612631]].<ref>PMID:2542324</ref> <ref>PMID:9432020</ref> <ref>PMID:12649162</ref>
[https://www.uniprot.org/uniprot/KAD1_HUMAN KAD1_HUMAN] Defects in AK1 are the cause of hemolytic anemia due to adenylate kinase deficiency (HAAKD) [MIM:[https://omim.org/entry/612631 612631].<ref>PMID:2542324</ref> <ref>PMID:9432020</ref> <ref>PMID:12649162</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KAD1_HUMAN KAD1_HUMAN]] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth.  
[https://www.uniprot.org/uniprot/KAD1_HUMAN KAD1_HUMAN] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Adenylate kinase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bunkoczi, G]]
[[Category: Bunkoczi G]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Filippakopoulos P]]
[[Category: Filippakopoulos, P]]
[[Category: Jansson A]]
[[Category: Jansson, A]]
[[Category: Knapp S]]
[[Category: Knapp, S]]
[[Category: Schreurs A]]
[[Category: Structural genomic]]
[[Category: Sundstrom M]]
[[Category: Schreurs, A]]
[[Category: Von Delft F]]
[[Category: Sundstrom, M]]
[[Category: Ap5a]]
[[Category: Diadenosine pentaphosphate]]
[[Category: Humna]]
[[Category: Nucleotide kinase]]
[[Category: Sgc]]
[[Category: Transferase]]

Latest revision as of 12:02, 14 February 2024

Crystal structure of human AK1A in complex with AP5ACrystal structure of human AK1A in complex with AP5A

Structural highlights

1z83 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

KAD1_HUMAN Defects in AK1 are the cause of hemolytic anemia due to adenylate kinase deficiency (HAAKD) [MIM:612631.[1] [2] [3]

Function

KAD1_HUMAN Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A. Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 1989 Jun 15;264(17):10148-55. PMID:2542324
  2. ↑ Qualtieri A, Pedace V, Bisconte MG, Bria M, Gulino B, Andreoli V, Brancati C. Severe erythrocyte adenylate kinase deficiency due to homozygous A-->G substitution at codon 164 of human AK1 gene associated with chronic haemolytic anaemia. Br J Haematol. 1997 Dec;99(4):770-6. PMID:9432020
  3. ↑ Corrons JL, Garcia E, Tusell JJ, Varughese KI, West C, Beutler E. Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic anemia. Blood. 2003 Jul 1;102(1):353-6. Epub 2003 Mar 20. PMID:12649162 doi:10.1182/blood-2002-07-2288

1z83, resolution 1.90Å

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