Cyclic Peptide DataBank (CPDB)

Summary

PDB ID	2XTT Go to RCSB ➚
Title	Bovine trypsin in complex with evolutionary enhanced Schistocerca gregaria protease inhibitor 1 (SGPI-1-P02)
Method	X-RAY DIFFRACTION
Resolution	0.93 Å
Release Date	2010-11-10
Authors	Wahlgren, W.Y.; Pal, G.; Kardos, J.; Porrogi, P.; Szenthe, B.; Patthy, A.; Graf, L.; Katona, G.
Source Organism	BOS TAURUS, SCHISTOCERCA GREGARIA
Keywords	HYDROLASE, CATALYTIC MECHANISM, INHIBITION, IN VITRO EVOLUTION
EC Number	3.4.21.4
Molecular Weight	27.36 kDa
Entity Count	Protein: 2, Nucleic Acid: 0, NA Hybrid: 0
Space Group	P 1 21 1
Cell Parameters	a=36.91 Å, b=63.61 Å, c=43.87 Å, α=90.00°, β=93.85°, γ=90.00°
Disulfide Bond	A4-A19;A14-A32;A17-A27
Other Links	Yes
Peptide Chains	A
Protein Chains	B
Peptide Lengths	36
Protein Lengths	223

Sequence Information

Chain: B - CATIONIC TRYPSIN (Length: 223)

1	IVGGYTCGAN TVPYQVSLNS GYHFCGGSLI NSQWVVSAAH CYKSGIQVRL GEDNINVVEG
61	NEQFISASKS IVHPSYNSNT LNNDIMLIKL KSAASLNSRV ASISLPTSCA SAGTQCLISG
121	WGNTKSSGTS YPDVLKCLKA PILSDSSCKS AYPGQITSNM FCAGYLEGGK DSCQGDSGGP
181	VVCSGKLQGI VSWGSGCAQK NKPGVYTKVC NYVSWIKQTI ASN

Chain: A - PROTEASE INHIBITOR SGPI-1 (Length: 36)

1	EQECEPGQTK KQDCNTCRCG SDGVWACTRM GCPPHA

References

The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action.

Wahlgren, W.Y., Pal, G., Kardos, J., Porrogi, P., Szenthe, B., Patthy, A., Graf, L., Katona, G.

J Biological Chem, 2011

PubMed: 21097875 | DOI: 10.1074/jbc.M110.161604

Ligand Information

ID	Name	Formula	Molecular Weight
CA	CALCIUM ION	Ca	40.078
ACT	ACETATE ION	C2 H3 O2	59.044

Biological Assemblies

Assembly ID: 1

Details: author_and_software_defined_assembly

Oligomeric State: Hetero 2-mer

Stoichiometry: A1, B1