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PDBsum entry 3olg

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protein ligands metals links
Hydrolase/hydrolase inhibitor PDB id
3olg
Jmol
Contents
Protein chain
495 a.a.
Ligands
SO4
HSD-G6D-GLC-HSD-
G6D-GLC-BGC
GLC-GLC-GLC-BGC
PCA
GLC
GLC-GLC-BGC
Metals
_CA
_CL
Waters ×263
PDB id:
3olg
Name: Hydrolase/hydrolase inhibitor
Title: Structures of human pancreatic alpha-amylase in complex with acarviostatin iii03
Structure: Pancreatic alpha-amylase. Chain: a. Synonym: pa, 1,4-alpha-d-glucan glucanohydrolase. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: amy2a. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
Resolution:
2.30Å     R-factor:   0.193     R-free:   0.216
Authors: X.Qin,L.Ren
Key ref: X.Qin et al. (2011). Structures of human pancreatic α-amylase in complex with acarviostatins: Implications for drug design against type II diabetes. J Struct Biol, 174, 196-202. PubMed id: 21111049
Date:
26-Aug-10     Release date:   13-Apr-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04746  (AMYP_HUMAN) -  Pancreatic alpha-amylase
Seq:
Struc:
511 a.a.
495 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.1  - Alpha-amylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   3 terms 
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
J Struct Biol 174:196-202 (2011)
PubMed id: 21111049  
 
 
Structures of human pancreatic α-amylase in complex with acarviostatins: Implications for drug design against type II diabetes.
X.Qin, L.Ren, X.Yang, F.Bai, L.Wang, P.Geng, G.Bai, Y.Shen.
 
  ABSTRACT  
 
No abstract given.