2ACH

CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS

Summary for 2ACH

• Entry DOI: 10.2210/pdb2ach/pdb
• Descriptor: ALPHA 1-ANTICHYMOTRYPSIN, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: proteinase inhibitor
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P01011 P01011
• Total number of polymer chains: 2
• Total formula weight: 46439.59

Authors

Baumann, U.,Huber, R.,Bode, W.,Grosse, D.,Lesjak, M.,Laurell, C.B. (deposition date: 1993-04-26, release date: 1993-07-15, Last modification date: 2024-11-06)

Primary citation

Baumann, U.,Huber, R.,Bode, W.,Grosse, D.,Lesjak, M.,Laurell, C.B.
Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7 A resolution and its comparison with other serpins.
J.Mol.Biol., 218:595-606, 1991

PubMed Abstract: The crystal structure of proteolytically modified human alpha 1-antichymotrypsin (ACT), a member of the serpin superfamily, has been solved by Paterson search techniques and refined to an R-factor of 18.0% at 2.7 A resolution with mean deviations from standard bond lengths and angles of 0.013 A and 3.1 degrees, respectively. The final model consists of 374 amino acid residues, 126 solvent molecules and five sugar residues. Asn70 could be identified unambiguously as a glycosylation site and Asn104 is probably also glycosylated. The structure of cleaved ACT is compared with cleaved alpha 1-antitrypsin (alpha 1 PI) and with plakalbumin, which are prototypical models for cleaved and intact serpins, respectively. Cleaved ACT is very similar to cleaved alpha 1 PI; in particular, it has strand s4A, which is liberated by proteolysis, inserted as the middle strand in beta-sheet A. ACT and alpha 1 PI differ locally only at sites of insertions, except at the segment s3C-turn-s4C, which is displaced by several angström units. This region of ACT is involved in DNA binding.

PubMed: 2016749
DOI: 10.1016/0022-2836(91)90704-A

Experimental method

X-RAY DIFFRACTION (2.7 Å)