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==Crystal structure of human AK1A in complex with AP5A==
==Crystal structure of human AK1A in complex with AP5A==
<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z83 FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='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='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='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='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='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'>[http://oca.weizmann.ac.il/oca-docs/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>
<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 ==
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</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=1z83 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=1z83 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Adenylate kinase]]
[[Category: Adenylate kinase]]
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Bunkoczi, G]]
[[Category: Bunkoczi, G]]
[[Category: Delft, F von]]
[[Category: Delft, F von]]

Revision as of 11:59, 20 January 2021

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 Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:AK1 (HUMAN)
Activity:Adenylate kinase, with EC number 2.7.4.3
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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