1h55
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1h55 |SIZE=350|CAPTION= <scene name='initialview01'>1h55</scene>, resolution 1.61Å | |PDB= 1h55 |SIZE=350|CAPTION= <scene name='initialview01'>1h55</scene>, resolution 1.61Å | ||
|SITE= <scene name='pdbsite=CAA:Hem+Binding+Site+For+Chain+A'>CAA</scene> | |SITE= <scene name='pdbsite=CAA:Hem+Binding+Site+For+Chain+A'>CAA</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h55 OCA], [http://www.ebi.ac.uk/pdbsum/1h55 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h55 RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Smith, A T.]] | [[Category: Smith, A T.]] | ||
[[Category: Szoke, H.]] | [[Category: Szoke, H.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: O]] | ||
[[Category: catalytic intermediate]] | [[Category: catalytic intermediate]] | ||
[[Category: compound ii]] | [[Category: compound ii]] | ||
| Line 39: | Line 38: | ||
[[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 20:57:54 2008'' |
Revision as of 17:57, 30 March 2008
| |||||||
| , resolution 1.61Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Peroxidase, with EC number 1.11.1.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF HORSERADISH PEROXIDASE C1A COMPOUND II
Overview
A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.
About this Structure
1H55 is a Single protein structure of sequence from Armoracia rusticana. Full crystallographic information is available from OCA.
Reference
The catalytic pathway of horseradish peroxidase at high resolution., Berglund GI, Carlsson GH, Smith AT, Szoke H, Henriksen A, Hajdu J, Nature. 2002 May 23;417(6887):463-8. PMID:12024218
Page seeded by OCA on Sun Mar 30 20:57:54 2008
