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Results 1 - 8 of 8
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EC Number Recommended Name Crystallization (Commentary) Organism Primary Accession No. Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.255protein O-GlcNAc transferase - Homo sapiens O15294 723250
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.255protein O-GlcNAc transferase a binary complex with UDP and a ternary complex with UDP and peptide substrate YPGGSTPVSSANMM, hanging drop vapor diffusion method Homo sapiens O15294 723266
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.255protein O-GlcNAc transferase cocrystallization of identified substrate peptides with OGT, derived from retinoblastoma-like protein 2 (RBL2411-422, KENPAVTPVSTA), proto-oncogene tyrosine protein kinase receptor Ret (Ret660-672, AQAFPVSYSSSGA), keratin-7 (KER77-19, SPVFTSRSAAFSC) and lamin B1 (LAMIN179-191, KLSPSPSSRVTVS). The peptide is teth­ered into a common binding mode by a combination of van der Waals interactions and hydrogen bonds that restrict torsional freedom in the -3 to +2 subsites only Homo sapiens O15294 736868
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.255protein O-GlcNAc transferase hybrid quantum mechanics/molecular mechanics analysis of reaction paths using alpha-phosphate and Asp554 as the catalytic bases. The mechanism with alpha-phosphate acting as the base is favorable. The reaction has a rate-limiting free energy barrier of 23.5 kcal/mol, whereas reactions utilizing Asp554 and water-assisted alpha-phosphate have barriers of 41.7 and 40.9 kcal/mol, respectively Homo sapiens O15294 736684
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.255protein O-GlcNAc transferase in complex with inhibitor goblin1, to 3.15 A resolution. UDP adopts the same conformation as observed in the OGT Michaelis complex and the peptide occupies the -4 to +2 subsites with a similar backbone conformation. The three-carbon linker connects the two components without introducing any strain, allowing both the UDP moiety and the peptide part of the inhibitor to adopt the optimal position in the binding site, mimicking the natural substrates Homo sapiens O15294 735633
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.255protein O-GlcNAc transferase three-dimensional structure of the protein domains I and II, conserved amino acid sequences Homo sapiens - 489612
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.255protein O-GlcNAc transferase vapour diffusion crystallisation experiments are performed Homo sapiens - 707093
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.255protein O-GlcNAc transferase X-ray crystallography Homo sapiens O15294 692070
Results 1 - 8 of 8
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