Biomaterial Database

Crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 A resolution. 2006

Irimpan I Mathews, and S Sri Krishna, and Robert Schwarzenbacher, and Daniel McMullan, and Polat Abdubek, and Eileen Ambing, and Jaume M Canaves, and Hsiu-Ju Chiu, and Ashley M Deacon, and Michael DiDonato, and Marc-André Elsliger, and Adam Godzik, and Carina Grittini, and Slawomir K Grzechnik, and Joanna Hale, and Eric Hampton, and Gye Won Han, and Justin Haugen, and Lukasz Jaroszewski, and Heath E Klock, and Eric Koesema, and Andreas Kreusch, and Peter Kuhn, and Scott A Lesley, and Inna Levin, and Mitchell D Miller, and Kin Moy, and Edward Nigoghossian, and Jessica Paulsen, and Kevin Quijano, and Ron Reyes, and Glen Spraggon, and Raymond C Stevens, and Henry van den Bedem, and Jeff Velasquez, and Aprilfawn White, and Guenter Wolf, and Qingping Xu, and Keith O Hodgson, and John Wooley, and Ian A Wilson

Synchrotron Radiation Laboratory, Stanford University, Menlo Park, California, USA.

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D017434	Protein Structure, Tertiary	The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure.	Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures
D018360	Crystallography, X-Ray	The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	X-Ray Crystallography,Crystallography, X Ray,Crystallography, Xray,X Ray Crystallography,Xray Crystallography,Crystallographies, X Ray,X Ray Crystallographies
D019733	Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor	Enzymes that catalyze the joining of glutamine-derived ammonia and another molecule. The linkage is in the form of a carbon-nitrogen bond. EC 6.3.5.	Carbon Nitrogen Ligases with Glutamine as Amide N Donor
D020124	Thermotoga maritima	A rod-shaped bacterium surrounded by a sheath-like structure which protrudes balloon-like beyond the ends of the cell. It is thermophilic, with growth occurring at temperatures as high as 90 degrees C. It is isolated from geothermally heated marine sediments or hot springs. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
D020836	Protein Structure, Quaternary	The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).	Quaternary Protein Structure,Protein Structures, Quaternary,Quaternary Protein Structures
D040681	Structural Homology, Protein	The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.	Protein Structural Homology,3-D Homologs, Protein,3-D Homology, Protein,3-Dimensional Homologs, Protein,3-Dimensional Homology, Protein,Homologs, 3-D, Protein,Homologs, 3-Dimensional, Protein,Homologs, Sturctural, Protein,Protein Structural Homologs,Structural Homologs, Protein,3 D Homologs, Protein,3 D Homology, Protein,3 Dimensional Homologs, Protein,3 Dimensional Homology, Protein,3-D Homolog, Protein,3-D Homologies, Protein,3-Dimensional Homolog, Protein,3-Dimensional Homologies, Protein,Homolog, Protein 3-D,Homolog, Protein 3-Dimensional,Homolog, Protein Structural,Homologies, Protein 3-D,Homologies, Protein 3-Dimensional,Homologies, Protein Structural,Homologs, Protein 3-D,Homologs, Protein 3-Dimensional,Homologs, Protein Structural,Homology, Protein 3-D,Homology, Protein 3-Dimensional,Homology, Protein Structural,Protein 3-D Homolog,Protein 3-D Homologies,Protein 3-D Homologs,Protein 3-D Homology,Protein 3-Dimensional Homolog,Protein 3-Dimensional Homologies,Protein 3-Dimensional Homologs,Protein 3-Dimensional Homology,Protein Structural Homolog,Protein Structural Homologies,Structural Homolog, Protein,Structural Homologies, Protein