1bm0

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[[Image:1bm0.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN==
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|PDB= 1bm0 |SIZE=350|CAPTION= <scene name='initialview01'>1bm0</scene>, resolution 2.50&Aring;
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<StructureSection load='1bm0' size='340' side='right'caption='[[1bm0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1bm0]] is a 2 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=1BM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BM0 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bm0 OCA], [https://pdbe.org/1bm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1bm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bm0 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Disease ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bm0 OCA], [http://www.ebi.ac.uk/pdbsum/1bm0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bm0 RCSB]</span>
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[https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:[https://omim.org/entry/103600 103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.<ref>PMID:8048949</ref> <ref>PMID:7852505</ref> <ref>PMID:9329347</ref> <ref>PMID:9589637</ref>
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}}
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== Function ==
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[https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.<ref>PMID:19021548</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/1bm0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1bm0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma (pHSA) or from a Pichia pastoris expression system (rHSA), was obtained from polyethylene glycol 4000 solution. Three-dimensional structures of pHSA and rHSA were determined at 2.5 A resolution from the new triclinic crystal form by molecular replacement, using atomic coordinates derived from a multiple isomorphous replacement work with a known tetragonal crystal form. The structures of pHSA and rHSA are virtually identical, with an r.m. s. deviation of 0.24 A for all Calpha atoms. The two HSA molecules involved in the asymmetric unit are related by a strict local twofold symmetry such that the Calpha atoms of the two molecules can be superimposed with an r.m.s. deviation of 0.28 A in pHSA. Cys34 is the only cysteine with a free sulfhydryl group which does not participate in a disulfide linkage with any external ligand. Domains II and III both have a pocket formed mostly of hydrophobic and positively charged residues and in which a very wide range of compounds may be accommodated. Three tentative binding sites for long-chain fatty acids, each with different surroundings, are located at the surface of each domain.
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'''CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN'''
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Crystal structure of human serum albumin at 2.5 A resolution.,Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K Protein Eng. 1999 Jun;12(6):439-46. PMID:10388840<ref>PMID:10388840</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1bm0" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma (pHSA) or from a Pichia pastoris expression system (rHSA), was obtained from polyethylene glycol 4000 solution. Three-dimensional structures of pHSA and rHSA were determined at 2.5 A resolution from the new triclinic crystal form by molecular replacement, using atomic coordinates derived from a multiple isomorphous replacement work with a known tetragonal crystal form. The structures of pHSA and rHSA are virtually identical, with an r.m. s. deviation of 0.24 A for all Calpha atoms. The two HSA molecules involved in the asymmetric unit are related by a strict local twofold symmetry such that the Calpha atoms of the two molecules can be superimposed with an r.m.s. deviation of 0.28 A in pHSA. Cys34 is the only cysteine with a free sulfhydryl group which does not participate in a disulfide linkage with any external ligand. Domains II and III both have a pocket formed mostly of hydrophobic and positively charged residues and in which a very wide range of compounds may be accommodated. Three tentative binding sites for long-chain fatty acids, each with different surroundings, are located at the surface of each domain.
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*[[Albumin|Albumin]]
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*[[Albumin 3D structures|Albumin 3D structures]]
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==About this Structure==
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== References ==
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1BM0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM0 OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of human serum albumin at 2.5 A resolution., Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K, Protein Eng. 1999 Jun;12(6):439-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10388840 10388840]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kashima, A.]]
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[[Category: Kashima A]]
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[[Category: Kobayashi, K.]]
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[[Category: Kobayashi K]]
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[[Category: Mochizuki, S.]]
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[[Category: Mochizuki S]]
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[[Category: Noda, M.]]
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[[Category: Noda M]]
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[[Category: Sugio, S.]]
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[[Category: Sugio S]]
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[[Category: albumin]]
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[[Category: carrier protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:03:44 2008''
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Current revision

CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

PDB ID 1bm0

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