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PDBsum entry 3dhp

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protein ligands metals links
Hydrolase PDB id
3dhp
Jmol
Contents
Protein chain
496 a.a. *
Ligands
GLC
GLC-AGL
HMC
Metals
_CA
_CL
Waters ×444
* Residue conservation analysis
PDB id:
3dhp
Name: Hydrolase
Title: Probing the role of aromatic residues at the secondary saccharide binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding
Structure: Alpha-amylase 1. Chain: a. Synonym: 1,4-alpha-d-glucan glucanohydrolase 1, salivary alpha-amylase. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda.
Resolution:
1.50Å     R-factor:   0.170     R-free:   0.186
Authors: C.Ragunath,S.G.A Manuel,H.M.Sait,C.Kasinathan
Date:
18-Jun-08     Release date:   01-Jul-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04745  (AMY1_HUMAN) -  Alpha-amylase 1
Seq:
Struc:
511 a.a.
496 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 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   3 terms 
  Biochemical function     catalytic activity     7 terms