WHAT is PDB???
The Protein Data Bank (PDB) is a repository for the 3-D structural data of large biological molecules, such as proteins and nucleic acids. (See also crystallographic database). The data, typically obtained by X-ray crystallography or NMR spectroscopy and submitted by biologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations (PDBe, PDBj, and RCSB). The PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB.
The PDB is a key resource in areas of structural biology, such as structural genomics. Most major scientific journals, and some funding agencies, such as the NIH in the USA, now require scientists to submit their structure data to the PDB. If the contents of the PDB are thought of as primary data, then there are hundreds of derived (i.e., secondary) databases that categorize the data differently. For example, both SCOP and CATH categorize structures according to type of structure and assumed evolutionary relations; GO categorize structures based on genes.[1]
HISTORY...
The PDB originated as a grassroots effort.[1] In 1971, Walter Hamilton of the Brookhaven National Laboratory agreed to set up the data bank at Brookhaven. Upon Hamilton's death in 1973, Tom Koeztle took over direction of the PDB. In January 1994, Joel Sussman was appointed head of the PDB. In October 1998,[2] the PDB was transferred to the Research Collaboratory for Structural Bioinformatics (RCSB); the transfer was completed in June 1999. The new director was Helen M. Berman of Rutgers University (one of the member institutions of the RCSB).[3] In 2003, with the formation of the wwPDB, the PDB became an international organization. The founding members are PDBe (Europe), RCSB(USA), andPDBj (Japan). The BMRB joined in 2006. Each of the four members of wwPDB can act as deposition, data processing and distribution centers for PDB data. The data processing refers to the fact that wwPDB staff review and annotates each submitted entry. The data are then automatically checked for plausibility. (The source code for this validation software has been made available to the public at no charge.
FTSH peptidase...
image of ftsh peptidase
| Author | Tomaras, A.P., |
| Experiment | X-RAY DIFFRACTION with resolution of 2.00 Å |
| Chain | A |
| EC | 3.6.5.4 |
Gene Ontology
| Cellular component | protein complex (GO:0043234) |
| Biological process | protein polymerization (GO:0051258) |
THERMOLYSIN...
image of termolysin
| Author | Senda, M., Senda, T., Kidokoro, S. |
| Experiment | X-RAY DIFFRACTION with resolution of 1.70 Å |
| Chain | A |
| EC | 3.4.24.27 |
Gene Ontology
| Cellular component | extracellular region (GO:0005576) |
| Molecular function | metalloendopeptidase activity (GO:0004222) |
| Biological process | proteolysis (GO:0006508) |
LEUCYL AMINOPEPTIDASE...
image of leucyl aminopeptidase
| Author | |
| Experiment | X-RAY DIFFRACTION with resolution of 1.50 Å |
| Chain | A, B, C, D, E, F |
| EC | 3.4.24.27 |
Gene Ontology
| Cellular component | intracellular (GO:0005622) |
| Molecular function | aminopeptidase activity (GO:0004177) |
| Biological process | proteolysis (GO:0006508) |
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