PDBsum entry 1gcy

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protein metals links
Hydrolase PDB id
Jmol PyMol
Protein chain
415 a.a. *
_CA ×2
Waters ×222
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: High resolution crystal structure of maltotetraose-forming exo-amylase
Structure: Glucan 1,4-alpha-maltotetrahydrolase. Chain: a. Engineered: yes
Source: Pseudomonas stutzeri. Organism_taxid: 316. Strain: mo-19. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.60Å     R-factor:   0.259     R-free:   0.304
Authors: Y.Mezaki,Y.Katsuya,M.Kubota,Y.Matsuura
Key ref: Y.Mezaki et al. (2001). Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri. Biosci Biotechnol Biochem, 65, 222-225. PubMed id: 11272837
14-Aug-00     Release date:   30-Aug-00    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P13507  (AMT4_PSEST) -  Glucan 1,4-alpha-maltotetraohydrolase
548 a.a.
415 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Glucan 1,4-alpha-maltotetraohydrolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of 1,4-alpha-D-glucosidic linkages in amylaceous polysaccharides so as to remove successive maltotetraose residues from the non-reducing chain ends.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     metabolic process   3 terms 
  Biochemical function     catalytic activity     8 terms  


Biosci Biotechnol Biochem 65:222-225 (2001)
PubMed id: 11272837  
Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
Y.Mezaki, Y.Katsuya, M.Kubota, Y.Matsuura.
The intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri (G4-1), which has a raw starch binding domain, has been crystallized. The structure was identified (PDB entry 1GCY) by the molecular replacement method using the structure of its catalytic domain (G4-2). The result showed that the raw starch binding domain is in a disordered state, the corresponding electron densities being almost invisible. Superposition of these two enzyme forms showed evidence for the possible location of the raw starch binding domain (SBD). This crystal is a novel case, in that it forms a regular lattice incorporating flexibly bound SBD in the channel of crystal packing of the catalytic domains.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19682075 C.Christiansen, M.Abou Hachem, S.Janecek, A.Viksø-Nielsen, A.Blennow, and B.Svensson (2009).
The carbohydrate-binding module family 20--diversity, structure, and function.
  FEBS J, 276, 5006-5029.  
18186486 J.Arunachalam, and N.Gautham (2008).
Hydrophobic clusters in protein structures.
  Proteins, 71, 2012-2025.  
12581203 S.Janecek, B.Svensson, and E.A.MacGregor (2003).
Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.
  Eur J Biochem, 270, 635-645.  
12906828 X.Robert, R.Haser, T.E.Gottschalk, F.Ratajczak, H.Driguez, B.Svensson, and N.Aghajari (2003).
The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs.
  Structure, 11, 973-984.
PDB codes: 1ht6 1p6w
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