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PDBsum entry 5jqp

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
5jqp

 

 

 

 

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Contents
Protein chains
918 a.a.
131 a.a.
Ligands
TRS
Metals
_CA ×2
Waters ×655
PDB id:
5jqp
Name: Hydrolase
Title: Crystal structure of er glucosidase ii heterodimeric complex consisting of catalytic subunit and the binding domain of regulatory subunit
Structure: Alpha glucosidase-like protein. Chain: a. Engineered: yes. Glucosidase 2 subunit beta-like protein. Chain: b. Fragment: unp residues 21-162. Engineered: yes
Source: Chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719). Organism_taxid: 759272. Strain: dsm 1495 / cbs 144.50 / imi 039719. Gene: ctht_0064960. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: ctht_0046400.
Resolution:
2.20Å     R-factor:   0.155     R-free:   0.206
Authors: T.Satoh,T.Toshimori,M.Noda,S.Uchiyama,K.Kato
Key ref: T.Satoh et al. (2016). Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control. Protein Sci, 25, 2095-2101. PubMed id: 27576940 DOI: 10.1002/pro.3031
Date:
05-May-16     Release date:   14-Sep-16    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
G0SG42  (G0SG42_CHATD) -  alpha-glucosidase from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Seq:
Struc:
 
Seq:
Struc:
977 a.a.
918 a.a.
Protein chain
Pfam   ArchSchema ?
G0S9M2  (G0S9M2_CHATD) -  Glucosidase 2 subunit beta from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Seq:
Struc:
 
Seq:
Struc:
562 a.a.
131 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.2.1.20  - alpha-glucosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal, non-reducing 1,4-linked D-glucose residues with release of D-glucose.

 

 
DOI no: 10.1002/pro.3031 Protein Sci 25:2095-2101 (2016)
PubMed id: 27576940  
 
 
Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control.
T.Satoh, T.Toshimori, M.Noda, S.Uchiyama, K.Kato.
 
  ABSTRACT  
 
No abstract given.

 

 

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