1raz: Difference between revisions

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|PDB= 1raz |SIZE=350|CAPTION= <scene name='initialview01'>1raz</scene>, resolution 1.9&Aring;
|PDB= 1raz |SIZE=350|CAPTION= <scene name='initialview01'>1raz</scene>, resolution 1.9&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=BR:BROMIDE ION'>BR</scene>
|LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1raz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1raz OCA], [http://www.ebi.ac.uk/pdbsum/1raz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1raz RCSB]</span>
}}
}}


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==Overview==
==Overview==
The three-dimensional structure of human carbonic anhydrase II complexed with azide and with bromide was investigated crystallographically. Both of these non-protonated inhibitors replace the zinc and the 'deep' water, two catalytically important water molecules in the active site of the molecule. Both the azide and the bromide ions bind in a distorted tetrahedral manner 0.4 and 1.1 A from the zinc water position, respectively, but are in close contact (2.0 and 2.6 A, respectively) with the zinc ion.
The three-dimensional structure of human carbonic anhydrase II complexed with azide and with bromide was investigated crystallographically. Both of these non-protonated inhibitors replace the zinc and the 'deep' water, two catalytically important water molecules in the active site of the molecule. Both the azide and the bromide ions bind in a distorted tetrahedral manner 0.4 and 1.1 A from the zinc water position, respectively, but are in close contact (2.0 and 2.6 A, respectively) with the zinc ion.
==Disease==
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611492 611492]]


==About this Structure==
==About this Structure==
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[[Category: Jonsson, B M.]]
[[Category: Jonsson, B M.]]
[[Category: Liljas, A.]]
[[Category: Liljas, A.]]
[[Category: BR]]
[[Category: ZN]]
[[Category: lyase(oxo-acid)]]
[[Category: lyase(oxo-acid)]]


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Revision as of 23:25, 30 March 2008

File:1raz.jpg


PDB ID 1raz

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: ,
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE


OverviewOverview

The three-dimensional structure of human carbonic anhydrase II complexed with azide and with bromide was investigated crystallographically. Both of these non-protonated inhibitors replace the zinc and the 'deep' water, two catalytically important water molecules in the active site of the molecule. Both the azide and the bromide ions bind in a distorted tetrahedral manner 0.4 and 1.1 A from the zinc water position, respectively, but are in close contact (2.0 and 2.6 A, respectively) with the zinc ion.

About this StructureAbout this Structure

1RAZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The structure of human carbonic anhydrase II in complex with bromide and azide., Jonsson BM, Hakansson K, Liljas A, FEBS Lett. 1993 May 10;322(2):186-90. PMID:8482389

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