Domain annotation: [ InterPro ]
D6BQN2_9ROSI Unreviewed; 109 AA. Glutaredoxin GRX; Jatropha curcas.
Protein structure models are computational predictions which may contain errors.
The suitability of a specific model for a particular application is determined by
its accuracy (See also "Outcome of a Workshop on Applications of Protein Models
in Biomedical Research. Structure (2009) 17: 151-159.").
The sequence identity between target protein and template structure is
commonly seen as a first indicator for the expected accuracy of a model,
as confirmed by various studies.
This model is based on target-template sequence alignment of
60% sequence identity (C). Typically, target-template
sequence alignments of this degree of similarity are mainly correct.
Structural variation in templates, and incorrect reconstruction of loops
(insertions and deletions) are the main sources of model inaccuracies.
Validation of the model quality and analysis of the variability
among template structures is advised.
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Target - Template Alignment:
Identity computed with respect to: Model
Colored by: identical residues and amino acid property
id. residues .......AL.KAKE..SS..VVVFSKT.C..C..VK.L..Q.GA..K..ELD..SDG...
id. residues QSALA.WTG..TVPNVFIGGK.IGGCD.....H....L.PLL..A....
MVIEW Color Scheme used: CLUSTAL
Hydrophobic amino acids
Large hydrophobic amino acids
Negatively charged amino acids
Positively charged amino acids
Polar amino acids