1UCY

THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A ALPHA (RESIDUES 7-19). THREE COMPLEXES, ONE WITH EPSILON-THROMBIN AND TWO WITH ALPHA-THROMBIN

1UCY の概要

• エントリーDOI: 10.2210/pdb1ucy/pdb
• 分子名称: THROMBIN, FIBRINOPEPTIDE A-ALPHA, ... (6 entities in total)
• 機能のキーワード: complex (serine protease-coagulation), serine, protease, thrombin, complex (serine protease-coagulation) complex, complex (serine protease/coagulation)
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted, extracellular space: P00735 P00735 P00735 P00735; Secreted: P12803
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 110610.51

構造登録者

Martin, P.,Edwards, B. (登録日: 1996-08-30, 公開日: 1997-02-12, 最終更新日: 2023-11-15)

主引用文献

Martin, P.D.,Malkowski, M.G.,DiMaio, J.,Konishi, Y.,Ni, F.,Edwards, B.F.
Bovine thrombin complexed with an uncleavable analog of residues 7-19 of fibrinogen A alpha: geometry of the catalytic triad and interactions of the P1', P2', and P3' substrate residues.
Biochemistry, 35:13030-13039, 1996

PubMed Abstract: The crystal structure of the noncovalent complex of bovine thrombin and a fibrinogen-A alpha tridecapeptide substrate analog, G17 psi, in which the scissile bond amide nitrogen of Gly-17f has been replaced by a methylene carbon, has been determined at 2.3 A resolution with an R factor of 17.1%. The geometry of the active site indicates that the crystal structure is a close model of the true Michaelis complex. The three independently determined thrombin/G17 psi complexes in the crystal asymmetric unit reveal novel interactions for the P2' and P3' residues-Pro-18f and Arg-19f, respectively-on the carboxyl-terminal side of the scissile bond and confirm previously observed interactions of the P1 (Arg-16f) through P10 (Asp-7f) positions on the amino-terminal side. The thrombin S2' binding site for Pro-18f, as observed in all three complexes, differs from that predicted by modeling studies and is notable for including two carbonyl oxygens of the thrombin main chain. Arg-19f occupies two binding sites on thrombin, S3'A and S3'B, which have dramatically different placements for the arginyl side chain and carboxyl terminus.

PubMed: 8855938
DOI: 10.1021/bi960656y

実験手法

X-RAY DIFFRACTION (2.2 Å)