Structure-function relationships in human salivary alpha-amylase: role of aromatic residues in a secondary binding site
Ragunath, C., Manuel, S.G.A., Kasinathan, C., Ramasubbu, N.(2008) Biologia (Bratisl) 63: 1028-1034
Experimental Data Snapshot
Starting Model: experimental
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(2008) Biologia (Bratisl) 63: 1028-1034
Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Alpha-amylase 1 | 496 | Homo sapiens | Mutation(s): 1  Gene Names: AMY1A, AMY1 EC: 3.2.1.1 | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P0DUB6 (Homo sapiens) Explore P0DUB6  Go to UniProtKB:  P0DUB6 | |||||
GTEx:  ENSG00000237763  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P0DUB6 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 3 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
HMC Query on HMC | F [auth A] | 5-HYDROXYMETHYL-CHONDURITOL C7 H12 O5 PJPGMULJEYSZBS-VZFHVOOUSA-N | |||
CA Query on CA | D [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N | |||
CL Query on CL | E [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |
Modified Residues 1 Unique | |||||
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ID | Chains | Type | Formula | 2D Diagram | Parent |
PCA Query on PCA | A | L-PEPTIDE LINKING | C5 H7 N O3 | GLN |
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 52.282 | α = 90 |
b = 75.046 | β = 90 |
c = 135.013 | γ = 90 |
Software Name | Purpose |
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REFMAC | refinement |
ADSC | data collection |
HKL-2000 | data reduction |
HKL-2000 | data scaling |
REFMAC | phasing |