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. Author manuscript; available in PMC: 2012 Nov 1.
Published in final edited form as: Trends Biotechnol. 2011 Jul 2;29(11):577–585. doi: 10.1016/j.tibtech.2011.06.001

Table 1.

Structures of trypsin-like proteases and zymogens in the open (E, Z) and collapsed (E*, Z*) formsa

PDB ID Resolution (Å) Refs
Collapsed form
Protease – E*
1DST Complement factor D mutant S215W 2.0 (45)
1DSU, 1HFD Complement factor D 2.0, 2.3 (24, 26)
2XW9 Complement factor D mutant S195A 1.2 (25)
2XWA Complement factor D mutant R218A 2.8 (25)
1GVZ Prostate specific antigen 1.42 (46)
1LTO αI-tryptase 2.2 (49)
2F9Ob αI-tryptase mutant D216G 2.1 (29)
1RD3 Thrombin mutant E217K 2.5 (42)
1TQ0, 3EE0 Thrombin mutant W215A/E217A 2.8, 2.75 (43, 44)
2GP9, 3BEI Thrombin mutant D102N 1.87, 1.55 (38, 40)
3GIC Thrombin mutant Δ146-149e 1.55 (37)
3JZ2 Thrombin mutant N143P 2.4 (39)
3EDX, 3HK3, 3HK6 Murine thrombin mutant W215A/E217A 2.4, 1.94, 3.2 (43)
1TON Tonin 1.8 (47)
1YBW Hepatocyte growth factor activator 2.7 (50)
2B9L Prophenoloxidase activating factor II 2.0 (48)
3DFJ, 3E1X Prostasin 1.45, 1.7 (51, 52)
Zymogen – Z*
1CHG, 1EX3 Chymotrypsinogen 2.5, 3.0 (53, 54)
1DDJ, 1QRZ Plasminogen 2.0, 2.0 (55, 56)
1FDP Profactor D 2.1 (23)
1GVL Prokallikrein 6 1.8 (58)
1MD7 Complement profactor C1r 3.2 (60)
1MZA, 1MZD Progranzyme K 2.23, 2.9 (61)
1SGF α subunit of nerve growth factor 3.15 (62)
3NXP Prethrombin-1 2.2 (63)
Open form
Protease - E
1MD8 Complement factor C1r 2.8 (60)
1MH0, 1SGI Thrombin mutant R77aA 2.8, 2.3 (35, 36)
2PGB Thrombin mutant C191A/C220A 1.54 (34)
2OCV Murine thrombin 2.2 (64)
1NPM Neuropsin 2.1 (67)
2F9Ob αI-tryptase mutant D216G 2.1 (29)
2G51, 2G52 Trypsin 1.84, 1.84 (68)
2I6Q, 2I6S, 2ODP, 2ODQ Complement factor C2a 2.1, 2.7, 1.9, 2.3 (65, 66)
Zymogen - Z
1TGB, 1TGN Trypsinogen 1.8, 1.65 (69, 70)
1ZJK Zymogen of MASP-2 2.18 (72)
2F83 Coagulation factor XI 2.87 (73)
2OK5 Complement profactor B 2.3 (71)
a

Structures of TLPs not included in the Table are in the E form but feature Ca2+ bound to regions known to affect activity and stability, and/or acetate or sulfate bound at or near the catalytic residues. Examples of such structures are β trypsin, cationic trypsin, trypsins from Fusarium oxysporum and Streptomyces gryseus and kallikrein 7. New structures of these enzymes without Ca2+ or anionic ligands near the active site will enable unambiguous assignment of the E or E* form.

b

The structure of αI-tryptase mutant D216G documents both the E and E* conformations in a 3:1 ratio (29).