1AKS

CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN

Summary for 1AKS

• Entry DOI: 10.2210/pdb1aks/pdb
• Descriptor: ALPHA TRYPSIN, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase, serine protease
• Biological source: Sus scrofa (pig); More
• Cellular location: Secreted, extracellular space: P00761 P00761
• Total number of polymer chains: 2
• Total formula weight: 23549.60

Authors

Johnson, A.,Krishnaswamy, S.,Sundaram, P.V.,Pattabhi, V. (deposition date: 1996-07-24, release date: 1997-02-12, Last modification date: 2024-10-23)

Primary citation

Johnson, A.,Krishnaswamy, S.,Sundaram, P.V.,Pattabhi, V.
The first structure at 1.8 A resolution of an active autolysate form of porcine alpha-trysoin.
Acta Crystallogr.,Sect.D, 53:311-315, 1997

PubMed Abstract: The first crystal structure of an active autolysate form of porcine alpha-trypsin (APT), a two-chain molecule obtained from the limited autolysis of porcine beta-trypsin at position Lys145-Ser146, has been determined. APT crystallizes in space group P2(1)2(1)2(1) with one protein molecule in the asymmetric unit. The structure was solved by molecular replacement followed by refinement using X-PLOR to an R factor of 0.200 and an R(free) of 0.285 for 8.0-1.8 A data with r.m.s deviations from ideal values of 0.01 A and 1.7 degrees for bond lengths and bond angles, respectively. Comparison with inactive autolysate porcine epsilon-trypsin (EPT) and porcine beta-trypsin in complex with bittergourd trypsin inhibitor (MCT) revealed a small but systematic directional chain shift around the active-site residues from APT to EPT to MCT.

PubMed: 15299934
DOI: 10.1107/S0907444997000358

Experimental method

X-RAY DIFFRACTION (1.8 Å)