Phyre Home Retrieve Phyre Job Id
Emailmdejesus@rockefeller.edu
DescriptionRVBD1951c_(-)_2200197_2200493
DateMon Aug 5 13:25:04 BST 2019
Unique Job ID7e4eefc953613bf4
SequenceMKAGELRVNI ... Download FASTA
Job Typenormal
Job Expiry

Summary 

Top model
Image coloured by rainbow N → C terminus
Model dimensions (Å):X:19.724 Y:19.257 Z:23.173
Model (left) based on template d1ntha_
Top template information
Fold:TIM beta/alpha-barrel
Superfamily:Monomethylamine methyltransferase MtmB
Family:Monomethylamine methyltransferase MtmB
Confidence and coverage
Confidence: 13.2% Coverage: 11%
11 residues ( 11% of your sequence) have been modelled with 13.2% confidence by the single highest scoring template.
You may wish to submit your sequence to Phyrealarm. This will automatically scan your sequence every week for new potential templates as they appear in the Phyre2 library.
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Warning: 77% of your sequence is predicted disordered. Disordered regions cannot be meaningfully predicted.
3D viewing
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Sequence analysis 

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Secondary structure and disorder prediction [Show] 

Domain analysis [Show] 

Detailed template information [Hide] 

 

#
Template Alignment Coverage3D Model Confidence
% i.d. Template Information
1d1ntha_
13.2 45
Fold:TIM beta/alpha-barrel
Superfamily:Monomethylamine methyltransferase MtmB
Family:Monomethylamine methyltransferase MtmB
2c4iogD_
9.5 13
PDB header:unknown function
Chain: D: PDB Molecule:secreted protein esxb;
PDBTitle: the crystal structure of a secreted protein esxb (wild-type, in p212 space group) from bacillus anthracis str. sterne
3c5jvkB_
7.6 14
PDB header:hydrolase
Chain: B: PDB Molecule:uncharacterized protein;
PDBTitle: structural insights into a family 39 glycoside hydrolase from the gut2 symbiont bacteroides cellulosilyticus wh2.
4c1vjqB_
6.5 71
PDB header:structural genomics, de novo protein
Chain: B: PDB Molecule:designed protein;
PDBTitle: designed protein based on backbone conformation of2 procarboxypeptidase-a (1aye) with sidechains chosen for maximal3 predicted stability.

Binding site prediction 

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