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*
Residue conservation analysis
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| PDB id: |
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2alw
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| Name: |
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Hydrolase
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| Title: |
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Golgi alpha-mannosidase ii complex with noeuromycin
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 Structure: |
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Alpha-mannosidase ii. Chain: a. Fragment: catalytic domain. Synonym: mannosyl-oligosaccharide 1,3-1,6- alpha- mannosidase, man ii, golgi alpha-mannosidase ii, aman ii. Engineered: yes
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Source:
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Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: gmii. Expressed in: drosophila melanogaster. Expression_system_taxid: 7227. Expression_system_cell_line: s2 cells.
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UniProt:
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1108 a.a. |
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| Struc: |
1014 a.a.* |
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| Key: |
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PfamA domain |
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PfamB domain |
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Secondary structure |
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CATH domain |
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* PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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Reaction:
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Hydrolysis of the terminal 1,3- and 1,6-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man(5)(GlcNAc)(3).
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Pathway:
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Resolution:
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1.86Å
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R-factor:
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0.141
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R-free:
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0.181
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Authors:
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D.A.Kuntz,M.B.Bols,H.Liu,D.R.Rose
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Key ref:
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[PubMed id: ]
d.a.kuntz
et al.
(2006).
The role of the active site Zn in the catalytic mechanism of the GH38 Golgi alpha-mannosidase II: implications from noeuromycin inhibition.
Biocatal.Biotransfor.,
34,
55-61.
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Date:
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08-Aug-05
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Release date:
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04-Jul-06
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Related entries:
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... plus others (see )
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