PDBsum entry 1r0t

Hydrolase/protein binding

PDB id

1r0t

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Contents

			Protein chains

					223 a.a.


					62 a.a.

			Ligands

					THR-ASN-GLU-GLU- GLY-LYS-ASP

			Waters ×128

Superseded by:

1z7k

PDB id:

1r0t

Links
- PDBe
- RCSB
- MMDB
- JenaLib
- Proteopedia
- CATH
- SCOP
- PDBSWS
- PDBePISA
- CSA
- ProSAT

Name:

Hydrolase/protein binding

Title:

Crystal structure of trypsin-second domain of the ovomucoid turkey egg white inhibitor complex

Structure:

Trypsin. Chain: a. Ovomucoid. Chain: b. Fragment: second domain. Ovomucoid. Chain: c. Fragment: first domain

Source:

Sus scrofa. Pig. Tissue: pancreas. Meleagris gallopavo. Common turkey. Tissue: egg white. Tissue: egg white

Biol. unit:

Trimer (from PQS)

Resolution:

1.90Å

R-factor:

0.195

R-free:

0.215

Authors:

B.Syed Ibrahim,V.Pattabhi

Key ref:

B.S.Ibrahim and V.Pattabhi (2004). Crystal structure of trypsin-turkey egg white inhibitor complex. Biochem Biophys Res Commun, 313, 8. PubMed id: 14672690 DOI: 10.1016/j.bbrc.2003.11.082

Date:

23-Sep-03

Release date:

23-Dec-03

PROCHECK

	Headers

	References

Protein chain

P00761 (TRYP_PIG) - Trypsin from Sus scrofa

Seq: Struc:					231 a.a. 223 a.a.

Protein chain

P01004 (IOVO_MELGA) -

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

Chain A: E.C.3.4.21.4 - trypsin.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

DOI no: 10.1016/j.bbrc.2003.11.082	Biochem Biophys Res Commun 313:8 (2004)
PubMed id: 14672690

Crystal structure of trypsin-turkey egg white inhibitor complex.
B.S.Ibrahim, V.Pattabhi.

ABSTRACT

Crystal structure of the complex between porcine beta-trypsin and the second domain of the Kazal-type ovomucoid turkey egg white trypsin inhibitor (OMTKY2) has been determined at 1.9A resolution. A peptide fragment from the first domain has been crystallized with the complex. Restrained-refinement of the structure led to an R-factor of 0.19 for the 32206 reflections. OMTKY2 exhibits the canonical Kazal-type fold with a central alpha-helix and a short two-stranded anti-parallel beta-sheet. The carbonyl carbon of the reactive site prefers trigonal geometry. The reactive site loop geometry of the inhibitor is complementary to the surface and charge of the binding site in beta-trypsin.