2KNT

THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5

Summary for 2KNT

• Entry DOI: 10.2210/pdb2knt/pdb
• Descriptor: COLLAGEN, PHOSPHATE ION (3 entities in total)
• Functional Keywords: kunitz inhibitor, extracellular matrix, connective tissue
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix (By similarity): P12111
• Total number of polymer chains: 1
• Total formula weight: 6734.48

Authors

Merigeau, K.,Arnoux, B.,Ducruix, A. (deposition date: 1997-01-15, release date: 1997-05-15, Last modification date: 2024-10-23)

Primary citation

Merigeau, K.,Arnoux, B.,Perahia, D.,Norris, K.,Norris, F.,Ducruix, A.
1.2 A refinement of the Kunitz-type domain from the alpha3 chain of human type VI collagen.
Acta Crystallogr.,Sect.D, 54:306-312, 1998

PubMed Abstract: The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain was previously described at 1.6 A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2 A. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (chi1 = -60 degrees). The solvent molecules and a phosphate ion are well ordered with an average B of 38 A2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure.

PubMed: 9761897
DOI: 10.1107/S0907444997010846

Experimental method

X-RAY DIFFRACTION (1.2 Å)