PDBsum entry 1sbw

Hydrolase/hydrolase inhibitor

PDB id: 1sbw

Contents

Protein chains

223 a.a. *

15 a.a. *

Ligands

SO4

Metals

_CA

Waters ×272

* Residue conservation analysis

PDB id:

1sbw

Name:

Hydrolase/hydrolase inhibitor

Title:

Crystal structure of mung bean inhibitor lysine active fragment complex with bovine beta-trypsin at 1.8a resolution

Structure:

Protein (beta-trypsin). Chain: a. Protein (mung bean inhibitor lysin active fragment). Chain: i

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreatic. Vigna radiata. Organism_taxid: 157791

Biol. unit:

Dimer (from PQS)

Resolution:

1.80Å R-factor: 0.164 R-free: 0.196

Authors:

Q.Huang,Y.Zhu,C.Chi,Y.Tang

Key ref:

Y.Zhu et al. (1999). Crystal structure of mung bean inhibitor lysine active fragment complex with bovine beta-trypsin at 1.8A resolution. J Biomol Struct Dyn, 16, 1219-1224. PubMed id: 10447205 DOI: 10.1080/07391102.1999.10508329

Date:

29-Apr-99 Release date: 06-May-99

Protein chain

P00760  (TRY1_BOVIN) -  Serine protease 1 from Bos taurus

Seq: 246 a.a.

Struc: 223 a.a.

Protein chain

P01062  (IBB_VIGRR) -  Bowman-Birk type trypsin inhibitor from Vigna radiata var. radiata

Seq: 72 a.a.

Struc: 15 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

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

DOI no: 10.1080/07391102.1999.10508329

J Biomol Struct Dyn 16:1219-1224 (1999)

PubMed id: 10447205

Crystal structure of mung bean inhibitor lysine active fragment complex with bovine beta-trypsin at 1.8A resolution.

Y.Zhu, Q.Huang, C.Chi.

ABSTRACT

The crystal structure of the complex of mung bean inhibitor lysine active fragment with bovine beta-trypsin has been determined by X-ray crystallographic analysis at a resolution of 1.8 A. Refinement of the model of the complex converged at a final R value of 0.16. From the resulting electron density map, about one-third of the residues of the inhibitor were identified and two residues, at position P4 and P2' respectively, were found to be inconsistent with the sequence reported previously. The peptide chain of the inhibitor at the trypsin active site turns back sharply at Pro23I and forms a 9-residue reactive loop, which interacts with trypsin in a similar manner to the other families of inhibitors, suggesting an important and common role of these regions in exhibiting inhibitory activity.