PDBsum entry 2xtt

Hydrolase

PDB id: 2xtt

Contents

Protein chains

35 a.a. *

223 a.a. *

Ligands

ACT

Metals

_CA

Waters ×350

* Residue conservation analysis

PDB id:

2xtt

Name:

Hydrolase

Title:

Bovine trypsin in complex with evolutionary enhanced schistocerca gregaria protease inhibitor 1 (sgpi-1-p02)

Structure:

Protease inhibitor sgpi-1. Chain: a. Fragment: residues 20-54. Synonym: protease inhibitor sgpi-1, schistocerca gregaria trypsin inhibitor, protease inhibitor sgpi-2, schistocerca gregaria chymotrypsin inhibitor, sgti, sgci. Engineered: yes. Other_details: in vitro evolved sequence with the following. Cationic trypsin.

Source:

Synthetic: yes. Schistocerca gregaria. Desert locust. Organism_taxid: 7010. Bos taurus. Bovine. Organism_taxid: 9913. Organ: pancreas. Tissue: glandular.

Resolution:

0.93Å R-factor: 0.117 R-free: 0.140

Authors:

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

Key ref:

W.Y.Wahlgren et al. (2011). 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. J Biol Chem, 286, 3587-3596. PubMed id: 21097875

Date:

12-Oct-10 Release date: 10-Nov-10

Protein chain

O46162  (SGP1_SCHGR) -  Serine protease inhibitor I/II from Schistocerca gregaria

Seq: 92 a.a.

Struc: 35 a.a.*

Protein chain

P00760  (TRY1_BOVIN) -  Serine protease 1 from Bos taurus

Seq: 246 a.a.

Struc: 223 a.a.

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain B: E.C.3.4.21.4 - trypsin.
• Reaction: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

J Biol Chem 286:3587-3596 (2011)

PubMed id: 21097875

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.

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

ABSTRACT

No abstract given.