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2j55
From Proteopedia
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|PDB= 2j55 |SIZE=350|CAPTION= <scene name='initialview01'>2j55</scene>, resolution 2.15Å | |PDB= 2j55 |SIZE=350|CAPTION= <scene name='initialview01'>2j55</scene>, resolution 2.15Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+L'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+L'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Amine_dehydrogenase Amine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.3 1.4.99.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Amine_dehydrogenase Amine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.3 1.4.99.3] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j55 OCA], [http://www.ebi.ac.uk/pdbsum/2j55 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j55 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pearson, A R.]] | [[Category: Pearson, A R.]] | ||
[[Category: Wilmot, C M.]] | [[Category: Wilmot, C M.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: GOL]] | ||
[[Category: copper]] | [[Category: copper]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| Line 37: | Line 38: | ||
[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:53:03 2008'' |
Revision as of 00:53, 31 March 2008
| |||||||
| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Amine dehydrogenase, with EC number 1.4.99.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE O-QUINONE IN COMPLEX WITH AMICYANIN.
Overview
X-ray exposure during crystallographic data collection can result in unintended redox changes in proteins containing functionally important redox centers. In order to directly monitor X-ray-derived redox changes in trapped oxidative half-reaction intermediates of Paracoccus denitrificans methylamine dehydrogenase, a commercially available single-crystal UV/Vis microspectrophotometer was installed on-line at the BioCARS beamline 14-BM-C at the Advanced Photon Source, Argonne, USA. Monitoring the redox state of the intermediates during X-ray exposure permitted the creation of a general multi-crystal data collection strategy to generate true structures of each redox intermediate.
About this Structure
2J55 is a Protein complex structure of sequences from Paracoccus denitrificans. Full crystallographic information is available from OCA.
Reference
Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry., Pearson AR, Pahl R, Kovaleva EG, Davidson VL, Wilmot CM, J Synchrotron Radiat. 2007 Jan;14(Pt 1):92-8. Epub 2006 Dec 15. PMID:17211075
Page seeded by OCA on Mon Mar 31 03:53:03 2008
