1ibq
From Proteopedia
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| - | [[Image:1ibq.jpg|left|200px]] | + | [[Image:1ibq.jpg|left|200px]] |
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| - | '''ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS''' | + | {{Structure |
| + | |PDB= 1ibq |SIZE=350|CAPTION= <scene name='initialview01'>1ibq</scene>, resolution 2.14Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspergillopepsin_I Aspergillopepsin I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.18 3.4.23.18] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IBQ is a [ | + | 1IBQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_phoenicis Aspergillus phoenicis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBQ OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases., Cho SW, Kim N, Choi MU, Shin W, Acta Crystallogr D Biol Crystallogr. 2001 Jul;57(Pt 7):948-56. Epub 2001, Jun 21. PMID:[http:// | + | Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases., Cho SW, Kim N, Choi MU, Shin W, Acta Crystallogr D Biol Crystallogr. 2001 Jul;57(Pt 7):948-56. Epub 2001, Jun 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11418762 11418762] |
[[Category: Aspergillopepsin I]] | [[Category: Aspergillopepsin I]] | ||
[[Category: Aspergillus phoenicis]] | [[Category: Aspergillus phoenicis]] | ||
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[[Category: aspergillopepsin]] | [[Category: aspergillopepsin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:12 2008'' |
Revision as of 09:48, 20 March 2008
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| , resolution 2.14Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aspergillopepsin I, with EC number 3.4.23.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS
Overview
The crystal structure of aspergillopepsin I (AP) from Aspergillus phoenicis has been determined at 2.18 A resolution and refined to R and R(free) factors of 21.5 and 26.0%, respectively. AP has the typical two beta-barrel domain structure of aspartic proteinases. The structures of the two independent molecules are partly different, exemplifying the flexible nature of the aspartic proteinase structure. Notably, the 'flap' in one molecule is closer, with a largest separation of 4.0 A, to the active site than in the other molecule. AP is most structurally homologous to penicillopepsin (PP) and then to endothiapepsin (EP), which share sequence identities of 68 and 56%, respectively. However, AP is similar to EP but differs from PP in the combined S1'-S2 subsite that is delineated by a flexible psi-loop in the C-terminal domain. The S1' and S2 subsites are well defined and small in AP, while there is no definite border between S1' and S2 and the open space for the S2 subsite is larger in PP. Comparison of the structures indicates that the two amino-acid residues equivalent to Leu295 and Leu297 of AP are the major determining factors in shaping the S1'-S2 subsite in the fungal aspartic proteinases.
About this Structure
1IBQ is a Single protein structure of sequence from Aspergillus phoenicis. Full crystallographic information is available from OCA.
Reference
Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases., Cho SW, Kim N, Choi MU, Shin W, Acta Crystallogr D Biol Crystallogr. 2001 Jul;57(Pt 7):948-56. Epub 2001, Jun 21. PMID:11418762
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