Crystal structure of the complex of sheep signalling glycoprotein with chitin trimer at 3.0A resolution
The structure was published by Srivastava, D.B., Ethayathulla, A.S., Kumar, J., et al., Sharma, S., Dey, S., and Singh, T.P., in 2007 in a paper entitled "Carbohydrate binding properties and carbohydrate induced conformational switch in sheep secretory glycoprotein (SPS-40): crystal structures of four complexes of SPS-40 with chitin-like oligosaccharides" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2006.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of SIGNAL PROCESSING PROTEIN. This molecule has the UniProt identifier Q6TMG6 (CH3L1_SHEEP). The sample contained 361 residues which is 100% of the natural sequence. Out of 361 residues 361 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: