1qfx
From Proteopedia
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|PDB= 1qfx |SIZE=350|CAPTION= <scene name='initialview01'>1qfx</scene>, resolution 2.4Å | |PDB= 1qfx |SIZE=350|CAPTION= <scene name='initialview01'>1qfx</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfx OCA], [http://www.ebi.ac.uk/pdbsum/1qfx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qfx RCSB]</span> | ||
}} | }} | ||
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[[Category: Loon, A P.G M.Van.]] | [[Category: Loon, A P.G M.Van.]] | ||
[[Category: Wyss, M.]] | [[Category: Wyss, M.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: SO4]] | ||
[[Category: phosphomonoesterase]] | [[Category: phosphomonoesterase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:59 2008'' |
Revision as of 20:13, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Activity: | 3-phytase, with EC number 3.1.3.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER
Overview
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.
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
Page seeded by OCA on Sun Mar 30 23:12:59 2008
