1gzb
From Proteopedia
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|PDB= 1gzb |SIZE=350|CAPTION= <scene name='initialview01'>1gzb</scene>, resolution 1.8Å | |PDB= 1gzb |SIZE=350|CAPTION= <scene name='initialview01'>1gzb</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=CA1:Ca+Binding+Site'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Binding+Site'>CA2</scene> and <scene name='pdbsite=GL1:Sugar+Binding+Site'>GL1</scene> | |SITE= <scene name='pdbsite=CA1:Ca+Binding+Site'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Binding+Site'>CA2</scene> and <scene name='pdbsite=GL1:Sugar+Binding+Site'>GL1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1gzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gzb OCA], [http://www.ebi.ac.uk/pdbsum/1gzb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gzb RCSB]</span> | ||
}} | }} | ||
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[[Category: Fukuyama, K.]] | [[Category: Fukuyama, K.]] | ||
[[Category: Kunishima, N.]] | [[Category: Kunishima, N.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: HEM]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
[[Category: heme]] | [[Category: heme]] | ||
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[[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 20:54:28 2008'' |
Revision as of 17:54, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , , | ||||||
| Activity: | Peroxidase, with EC number 1.11.1.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEROXIDASE
Overview
In the presence of ammonium sulfate the absorption spectra of a peroxidase from the fungus Arthromyces ramosus (ARP) showed that the low-spin component increased as the pH increased from 6.0 to 9.0, whereas in its absence ARP remained in the high-spin state in the pH range investigated. The crystal structure of ARP at pH 4.5 in the presence of ammonium sulfate at 1.8 A resolution showed that the electron density at the 6th position of the heme iron seen at pH 7.5 had disappeared and that the iron atom deviated markedly from the heme plane. These observations strongly suggest that under physiological conditions the heme of ARP is in the pentacoordinated high-spin state and that at a high pH the heme iron is able to bind ammonia, forming the low-spin state. The location of the water molecule at the distal side of the heme in peroxidases is also discussed.
About this Structure
1GZB is a Single protein structure of sequence from Eukaryota. Full crystallographic information is available from OCA.
Reference
Pentacoordination of the heme iron of Arthromyces ramosus peroxidase shown by a 1.8 A resolution crystallographic study at pH 4.5., Kunishima N, Amada F, Fukuyama K, Kawamoto M, Matsunaga T, Matsubara H, FEBS Lett. 1996 Jan 15;378(3):291-4. PMID:8557120
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