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1hfu
From Proteopedia
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|PDB= 1hfu |SIZE=350|CAPTION= <scene name='initialview01'>1hfu</scene>, resolution 1.68Å | |PDB= 1hfu |SIZE=350|CAPTION= <scene name='initialview01'>1hfu</scene>, resolution 1.68Å | ||
|SITE= <scene name='pdbsite=T1:Type+3+Cu+Binding+Site'>T1</scene> | |SITE= <scene name='pdbsite=T1:Type+3+Cu+Binding+Site'>T1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfu OCA], [http://www.ebi.ac.uk/pdbsum/1hfu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hfu RCSB]</span> | ||
}} | }} | ||
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[[Category: Davies, G J.]] | [[Category: Davies, G J.]] | ||
[[Category: Ducros, V.]] | [[Category: Ducros, V.]] | ||
| - | [[Category: CU]] | ||
[[Category: blue multi-copper oxidase]] | [[Category: blue multi-copper oxidase]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| Line 34: | Line 36: | ||
[[Category: type-2 copper depleted]] | [[Category: type-2 copper depleted]] | ||
| - | ''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 21:04:12 2008'' |
Revision as of 18:04, 30 March 2008
| |||||||
| , resolution 1.68Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Laccase, with EC number 1.10.3.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS AT 1.68 A RESOLUTION
Overview
Laccases (E.C. 1.10.3.2; benzenediol oxygen oxidoreductases) couple the four-electron reduction of dioxygen to water to four one-electron oxidations of a reducing substrate. The three-dimensional structure of the 'blue' multi-copper oxidase laccase from the fungus Coprinus cinereus at 1.68 A reveals the structural basis for isoforms of the type 2 Cu-depleted species.
About this Structure
1HFU is a Single protein structure of sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA.
Reference
Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms., Ducros V, Brzozowski AM, Wilson KS, Ostergaard P, Schneider P, Svendson A, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):333-6. PMID:11173497
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