1npx: Difference between revisions
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|PDB= 1npx |SIZE=350|CAPTION= <scene name='initialview01'>1npx</scene>, resolution 2.16Å | |PDB= 1npx |SIZE=350|CAPTION= <scene name='initialview01'>1npx</scene>, resolution 2.16Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CYO:OXYGENS+BOUND+TO+CYS+SG'>CYO</scene> | |LIGAND= <scene name='pdbligand=CYO:OXYGENS+BOUND+TO+CYS+SG'>CYO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1npx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npx OCA], [http://www.ebi.ac.uk/pdbsum/1npx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1npx RCSB]</span> | |||
}} | }} | ||
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[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
[[Category: Stehle, T.]] | [[Category: Stehle, T.]] | ||
[[Category: oxidoreductase(h2o2(a))]] | [[Category: oxidoreductase(h2o2(a))]] | ||
''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 22:33:52 2008'' | ||
Revision as of 22:33, 30 March 2008
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| , resolution 2.16Å | |||||||
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| Ligands: | , | ||||||
| Activity: | NADH peroxidase, with EC number 1.11.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION
OverviewOverview
The crystal structure of NADH peroxidase (EC 1.11.1.1) from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been refined to a resolution of 2.16 A using the simulated annealing method. The final crystallographic R-factor is 17.7% for all data in the resolution range 7 to 2.16 A. The standard deviations are 0.015 A in bond lengths and 3.0 degrees in bond angles for the final model, which includes all 447 amino acid residues, one FAD and 369 water molecules. The enzyme is a symmetrical tetramer with point group D2; the symmetry is crystallographic. The redox center of the enzyme consists of FAD and a cysteine (Cys42), which forms a sulfenic acid (Cys-SOH) in its oxidized state. A histidine (His10) close to Cys42 is likely to act as an active-site base. In the analyzed crystal, the enzyme was in a non-native oxidation state with Cys42 oxidized to a sulfonic acid Cys-SO3H. The chain fold of NADH peroxidase is similar to those of disulfide oxidoreductases. A comparison with glutathione reductase, a representative of this enzyme family, is given.
About this StructureAbout this Structure
1NPX is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.
ReferenceReference
Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution., Stehle T, Ahmed SA, Claiborne A, Schulz GE, J Mol Biol. 1991 Oct 20;221(4):1325-44. PMID:1942054
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