Sandbox Reserved 1098: Difference between revisions
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
This protein has four principal domains on a single peptide chain: a A-domain, a catalytic domain and two substrate binding domains[ | This protein has four principal domains on a single peptide chain: a A-domain, a catalytic domain and two substrate binding domains[http://www.uniprot.org/uniprot/Q86W56]. | ||
The first 456 amino acids of the peptide chain form the A-domain. Then from 610 to 795 amino acids is located the catalytic domain. This catalytic domain can binding with other proteins with two amino acids (the 726 and 727 amino acids). Next the second substrate binding domain is located from the 869 th to the 874th amino acids. [https://www.uniprot.org/uniprot/Q86W56] | The first 456 amino acids of the peptide chain form the A-domain. Then from 610 to 795 amino acids is located the catalytic domain. This catalytic domain can binding with other proteins with two amino acids (the 726 and 727 amino acids). Next the second substrate binding domain is located from the 869 th to the 874th amino acids. [https://www.uniprot.org/uniprot/Q86W56] | ||
So, most of the amino acids form the A-domain and the catzlytic domain and only few amino acids (8 a.a) make links with other proteins. | So, most of the amino acids form the A-domain and the catzlytic domain and only few amino acids (8 a.a) make links with other proteins. | ||
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=== Secondary Structure === | === Secondary Structure === | ||
This protein is 37% helical and 13% beta sheet. Indeed, it has 25 helices on 198 residues and 23 strands on 74 residues. It has also few 3/10 helices. [ | This protein is 37% helical and 13% beta sheet. Indeed, it has 25 helices on 198 residues and 23 strands on 74 residues. It has also few 3/10 helices. [http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=6HMM] | ||
Involving the torsion angles the backbone and the sidechain have to be differentiated. Indeed none residue does't respect the Ramachandran's angle, whereas in sidechains where 2% of the residues are Ramachandran outliers because they have non-rotameric sidechains. [ | Involving the torsion angles the backbone and the sidechain have to be differentiated. Indeed none residue does't respect the Ramachandran's angle, whereas in sidechains where 2% of the residues are Ramachandran outliers because they have non-rotameric sidechains. [http://files.rcsb.org/pub/pdb/validation_reports/hm/6hmm/6hmm_full_validation.pdf] | ||
=== Quaternary Structure === | === Quaternary Structure === | ||
Poly(ADP-ribose)glycohydrolase interact with PCNA or NUDT5. When this protein is binding with NUDT5 it can remodeling chromatin.[ | Poly(ADP-ribose)glycohydrolase interact with PCNA or NUDT5. When this protein is binding with NUDT5 it can remodeling chromatin.[http://www.uniprot.org/uniprot/Q86W56] | ||
=== Links of PARG with other ligands === | === Links of PARG with other ligands === | ||
