Crystal Structure of the Human Rhesus Glycoprotein RhCG
The structure was published by Gruswitz, F., Chaudhary, S., Ho, J.D., et al., Sali, A., Westhoff, C.M., and Stroud, R.M., in 2010 in a paper entitled "Function of human Rh based on structure of RhCG at 2.1 A." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2009.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Ammonium transporter Rh type C. This molecule has the UniProt identifier Q9UBD6 (RHCG_HUMAN). The sample contained 490 residues which is 100% of the natural sequence. Out of 490 residues 403 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 most likely forms homotrimers.
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: