› 1nm9

X-ray diffraction
2.1Å resolution

Crystal structure of recombinant human salivary amylase mutant W58A

Released:
DOI: 10.2210/pdb1nm9/pdb
PDB entry 1nm9 coloured by chain, front view.
PDB entry 1nm9 coloured by chain, side view.
PDB entry 1nm9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human salivary alpha-amylase Trp58 situated at subsite -2 is critical for enzyme activity.
Ramasubbu N, Ragunath C, Mishra PJ, Thomas LM, Gyémánt G, Kandra L
Eur J Biochem 271 2517-29 (2004)
PMID: 15182367

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-amylase 1A Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.84 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P0DUB6 (Residues: 16-511; Coverage: 100%)
Gene names: AMY1, AMY1A
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, AGL
Carbohydrate polymer
4 bound ligands:
Ligand HMC 1 x HMC
Ligand GLC 1 x GLC
Ligand CA 1 x CA
Ligand CL 1 x CL
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 51.946Å b: 74.06Å c: 134.508Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.196
Expression system: Spodoptera frugiperda

Quick links

Citations

3 review citations

Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases.
Cuyvers et al. (2012)
2 more

1 mention without citation

'Hot' macromolecular crystals.
Koclega et al. (2009)