INTERACTION OF FACTOR XIII ACTIVATION PEPTIDE WITH ALPHA-THROMBIN: CRYSTAL STRUCTURE OF THE ENZYME-SUBSTRATE COMPLEX
The structure was published by Sadasivan, C. and Yee, V.C., in 2000 in a paper entitled "Interaction of the factor XIII activation peptide with alpha -thrombin. Crystal structure of its enzyme-substrate analog complex." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 3 biomacromolecules, namely ALPHA-THROMBIN (LIGHT CHAIN), ALPHA-THROMBIN (HEAVY CHAIN), and FACTOR XIII ACTIVATION PEPTIDE (28-37).
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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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: