1qgj
From Proteopedia
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|PDB= 1qgj |SIZE=350|CAPTION= <scene name='initialview01'>1qgj</scene>, resolution 1.90Å | |PDB= 1qgj |SIZE=350|CAPTION= <scene name='initialview01'>1qgj</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgj OCA], [http://www.ebi.ac.uk/pdbsum/1qgj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qgj RCSB]</span> | ||
}} | }} | ||
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[[Category: Oestergaard, L.]] | [[Category: Oestergaard, L.]] | ||
[[Category: Welinder, K G.]] | [[Category: Welinder, K G.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: GSH]] | ||
| - | [[Category: HEM]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''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 23:13:13 2008'' |
Revision as of 20:13, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ARABIDOPSIS THALIANA PEROXIDASE N
Overview
The structure of the neutral peroxidase from Arabidopsis thaliana (ATP N) has been determined to a resolution of 1.9 A and a free R value of 20.5%. ATP N has the expected characteristic fold of the class III peroxidases, with a C(alpha) r.m.s.d. of 0.82 A when compared with horseradish peroxidase C (HRP C). HRP C is 54% identical to ATP N in sequence. When the structures of four class III plant peroxidases are superimposed, the regions with structural differences are non-randomly distributed; all are located in one half of the molecule. The architecture of the haem pocket of ATP N is very similar to that of HRP C, in agreement with the low small-molecule substrate specificity of all class III peroxidases. The structure of ATP N suggests that the pH dependence of the substrate turnover will differ from that of HRP C owing to differences in polarity of the residues in the substrate-access channel. Since there are fewer hydrogen bonds to haem C17 propionate O atoms in ATP N than in HRP C, it is suggested that ATP N will lose haem more easily than HRP C. Unlike almost all other class III plant peroxidases, ATP N has a free cysteine residue at a similar position to the suggested secondary substrate-binding site in lignin peroxidase.
About this Structure
1QGJ is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
Arabidopsis thaliana peroxidase N: structure of a novel neutral peroxidase., Mirza O, Henriksen A, Ostergaard L, Welinder KG, Gajhede M, Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):372-5. PMID:10713531
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