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PDBsum entry 3trs

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3trs

 

 

 

 

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Contents
Protein chains
37 a.a.
171 a.a.
30 a.a.
Ligands
DMS ×2
Waters ×198
PDB id:
3trs
Name: Hydrolase
Title: The crystal structure of aspergilloglutamic peptidase from aspergillus niger
Structure: Aspergillopepsin-2 light chain. Chain: a, c. Synonym: aspergillopepsin ii light chain. Aspergillopepsin-2 heavy chain. Chain: b, d. Synonym: aspergillopepsin ii heavy chain. Ec: 3.4.23.19
Source: Aspergillus niger. Organism_taxid: 29838. Strain: var. Macrosporus. Strain: var. Macrosporus
Resolution:
1.60Å     R-factor:   0.210     R-free:   0.239
Authors: H.Sasaki,K.Kubota,W.C.Lee,J.Ohtsuka,M.Kojima,K.Takahashi,M.Tanokura
Key ref: H.Sasaki et al. (2012). The crystal structure of an intermediate dimer of aspergilloglutamic peptidase that mimics the enzyme-activation product complex produced upon autoproteolysis. J Biochem (tokyo), 152, 45-52. PubMed id: 22569035
Date:
10-Sep-11     Release date:   22-Aug-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P24665  (PRTA_ASPNG) -  Aspergillopepsin-2 from Aspergillus niger
Seq:
Struc:
282 a.a.
37 a.a.
Protein chains
Pfam   ArchSchema ?
P24665  (PRTA_ASPNG) -  Aspergillopepsin-2 from Aspergillus niger
Seq:
Struc:
282 a.a.
171 a.a.
Protein chain
Pfam   ArchSchema ?
P24665  (PRTA_ASPNG) -  Aspergillopepsin-2 from Aspergillus niger
Seq:
Struc:
282 a.a.
30 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.3.4.23.19  - aspergillopepsin Ii.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage in A chain of insulin: 3-Asn-|-Gln-4, 13-Gly-|-Ala-14, and 26-Tyr-|-Thr-27.

 

 
J Biochem (tokyo) 152:45-52 (2012)
PubMed id: 22569035  
 
 
The crystal structure of an intermediate dimer of aspergilloglutamic peptidase that mimics the enzyme-activation product complex produced upon autoproteolysis.
H.Sasaki, K.Kubota, W.C.Lee, J.Ohtsuka, M.Kojima, S.Iwata, A.Nakagawa, K.Takahashi, M.Tanokura.
 
  ABSTRACT  
 
No abstract given.

 

 

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