PDBsum entry 3qtl

Hydrolase/hydrolase inhibitor

PDB id: 3qtl

Contents

Protein chains

269 a.a.

75 a.a.

Waters ×157

PDB id:

3qtl

Name:

Hydrolase/hydrolase inhibitor

Title:

Structural basis for dual-inhibition mechanism of a non-classical kazal-type serine protease inhibitor from horseshoe crab in complex with subtilisin

Structure:

Subtilisin-like serin protease. Chain: a, b, c. Fragment: unp residues 106-379. Engineered: yes. Kazal-type serine protease inhibitor spi-1. Chain: d. Fragment: unp residues 24-99. Engineered: yes

Source:

Bacillus licheniformis. Organism_taxid: 1402. Gene: apre. Expressed in: escherichia coli. Expression_system_taxid: 562. Carcinoscorpius rotundicauda. Mangrove horseshoe crab. Organism_taxid: 6848. Gene: spi-1.

Resolution:

2.60Å R-factor: 0.204 R-free: 0.269

Authors:

R.T.Shenoy,J.Sivaraman

Key ref:

R.T.Shenoy et al. (2011). Structural basis for dual-inhibition mechanism of a non-classical Kazal-type serine protease inhibitor from horseshoe crab in complex with subtilisin. Plos One, 6, e18838. PubMed id: 21541315

Date:

23-Feb-11 Release date: 01-Jun-11

Protein chains

Q6PNN5  (Q6PNN5_BACLI) -  Alkaline protease from Bacillus licheniformis

Seq: 379 a.a.

Struc: 269 a.a.

Protein chain

A1X1V8  (A1X1V8_CARRO) -  Kazal-type serine protease inhibitor SPI-1 from Carcinoscorpius rotundicauda

Seq: 109 a.a.

Struc: 75 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C: E.C.3.4.21.62 - subtilisin.
• Reaction: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.

Plos One 6:e18838 (2011)

PubMed id: 21541315

Structural basis for dual-inhibition mechanism of a non-classical Kazal-type serine protease inhibitor from horseshoe crab in complex with subtilisin.

R.T.Shenoy, S.Thangamani, A.Velazquez-Campoy, B.Ho, J.L.Ding, J.Sivaraman.

ABSTRACT

No abstract given.