1qfx

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{{STRUCTURE_1qfx| PDB=1qfx | SCENE= }}
{{STRUCTURE_1qfx| PDB=1qfx | SCENE= }}
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'''PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER'''
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===PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER===
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==Overview==
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The crystal structure of Aspergillus niger pH 2.5 acid phosphatase (EC 3.1.3.2) has been determined at 2.4 A resolution. In the crystal, two dimers form a tetramer in which the active sites are easily accessible to substrates. The main contacts in the dimer come from the N termini, each lying on the surface of the neighbouring molecule. The monomer consists of two domains, with the active site located at their interface. The active site has a highly conserved catalytic center and a charge distribution, which explains the highly acidic pH optimum and the broad substrate specificity of the enzyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 10329192 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10329192}}
==About this Structure==
==About this Structure==
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[[Category: Wyss, M.]]
[[Category: Wyss, M.]]
[[Category: Phosphomonoesterase]]
[[Category: Phosphomonoesterase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:14:50 2008''

Revision as of 04:14, 28 July 2008

Image:1qfx.png

Template:STRUCTURE 1qfx

PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER

Template:ABSTRACT PUBMED 10329192

About this Structure

1QFX is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

Reference

Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution., Kostrewa D, Wyss M, D'Arcy A, van Loon AP, J Mol Biol. 1999 May 21;288(5):965-74. PMID:10329192

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