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Cathepsin E is an enzyme (EC 3.4.23.34) that in humans is encoded by the CTSE gene. [5] [6] [7] The enzyme is also known as slow-moving proteinase, erythrocyte membrane aspartic proteinase, SMP, EMAP, non-pepsin proteinase, cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme.
The PDBbind database is a comprehensive collection of experimentally measured binding affinity data (Kd, Ki, and IC50) for the protein-ligand complexes deposited in the Protein Data Bank (PDB). [ 1 ] [ 2 ] It thus provides a link between energetic and structural information of protein-ligand complexes, which is of great value to various studies ...
162,041 structures in the PDB have a structure factor file. 11,242 structures have an NMR restraint file. 5,774 structures in the PDB have a chemical shifts file. 13,388 structures in the PDB have a 3DEM map file deposited in EM Data Bank. Most structures are determined by X-ray diffraction, but about 7% of structures are determined by protein ...
20788 Ensembl ENSG00000198911 ENSMUSG00000022463 UniProt Q12772 Q3U1N2 RefSeq (mRNA) NM_004599 NM_033218 RefSeq (protein) NP_004590 NP_150087 Location (UCSC) Chr 22: 41.83 – 41.91 Mb Chr 15: 82.03 – 82.09 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Sterol regulatory element-binding protein 2 (SREBP-2) also known as sterol regulatory element binding transcription factor 2 ...
The alpha/beta hydrolase superfamily is a superfamily of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function that share a common fold. [1] The core of each enzyme is an alpha/beta-sheet (rather than a barrel ), containing 8 beta strands connected by 6 alpha helices .
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As of February 2015, SCOPe 2.05 classified 71,000 of the 110,000 total PDB entries. [ 11 ] SCOP2 prototype was a beta version of Structural classification of proteins and classification system that aimed to more the evolutionary complexity inherent in protein structure evolution. [ 12 ]
[3] [10] [9] Many papain-like protease enzymes function as monomers, though a few, such as cathepsin C (Dipeptidyl-peptidase I), are homotetramers. The mature monomer structure is characteristically divided into two lobes or subdomains, known as the L-domain ( N-terminal ) and the R-domain ( C-terminal ), where the active site is located ...