HUMAN FACTOR XIII WITH CALCIUM BOUND IN THE ION SITE
The structure was published by Garzon, R.J., Pratt, K.P., Bishop, P.D., Le Trong, I., Stenkamp, R.E., and Teller, D.C., in in a paper entitled "Tryptophan 279 is Essential for the Transglutaminase Activity of Coagulation Factor XIII: Functional and Structural Characterization" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.01 Å and deposited in 2000.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of COAGULATION FACTOR XIII.
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 homodimers.
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: