Molecular Playground/ERMan1: Difference between revisions

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  {{STRUCTURE_1x9d|  PDB=1x9d  | SIZE=300| SCENE= |right|  CAPTION=α-mannosidase complex with mannopyranoside, sulfate, 1,4-butanediol, Ca+2 ion, [[1x9d]] }}
  {{STRUCTURE_1x9d|  PDB=1x9d  | SIZE=300| SCENE= |right|  CAPTION=Human α-mannosidase class I complex with mannopyranoside, sulfate, 1,4-butanediol, Ca+2 ion, [[1x9d]] }}


"Molecular Playground banner: A catalytic timer for protein degradation."
"Molecular Playground banner: A catalytic timer for protein degradation."
==3D structures of mannosidases==
[[Mannosidase]]


[http://proteopedia.org/wiki/index.php/CBI_Molecules]
[http://proteopedia.org/wiki/index.php/CBI_Molecules]
[http://proteopedia.org/wiki/index.php/1x9d]
[http://proteopedia.org/wiki/index.php/1x9d]

Latest revision as of 13:25, 24 July 2011

ERMan1ERMan1

Alpha-mannosidases I(ERMan1) is a human protein that resides in the endoplasmic reticulum(ER). ERMan1 is a member of the class 1 glycosylhydrolase family 47 group proteins and sports a Tim-barrel fold. Asparagine(N)-linked glycans are common covalent modifiers in the ER that aid in protein folding and trafficking. ERMan1 trims N-linked glycans to target a misfolded protein for degradation. The slow acting kinetics of ERMan1 have been proposed to act as a timer for protein degradation, creating a discrete window for protein folding followed by degradation if the substrate protein cannot reach the native state.




PDB ID 1x9d

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Human α-mannosidase class I complex with mannopyranoside, sulfate, 1,4-butanediol, Ca+2 ion, 1x9d
Ligands: , , ,
Gene: MAN1B1 (Homo sapiens)
Activity: Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113
Related: 1fmi
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



"Molecular Playground banner: A catalytic timer for protein degradation."

3D structures of mannosidases3D structures of mannosidases

Mannosidase

[1] [2]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Johan Sunryd, Michal Harel