PDBsum entry 4zv7

Hydrolase

PDB id: 4zv7

Contents

Protein chain

317 a.a.

Ligands

NAG-NAG

Waters ×332

PDB id:

4zv7

Name:

Hydrolase

Title:

Crystal structure of hexagonal form of lipase b from candida antarctica

Structure:

Lipase b. Chain: a. Fragment: unp residues 26-342. Synonym: calb. Engineered: yes

Source:

Candida antarctica. Yeast. Organism_taxid: 34362. Expressed in: aspergillus oryzae. Expression_system_taxid: 5062

Resolution:

2.00Å R-factor: 0.147 R-free: 0.193

Authors:

P.Strzelczyk,J.Blaszczyk,G.Bujacz

Key ref:

P.Strzelczyk et al. (2016). Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica. Acta Biochim Pol, 63, 1065-109. PubMed id: 26716135 DOI: 10.18388/abp.2015_1065

Date:

18-May-15 Release date: 13-Jan-16

Protein chain

P41365  (LIPB_PSEA2) -  Lipase B from Pseudozyma antarctica

Seq: 342 a.a.

Struc: 317 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.1.3 - triacylglycerol lipase.
• Reaction: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.18388/abp.2015_1065

Acta Biochim Pol 63:1065-109 (2016)

PubMed id: 26716135

Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.

P.Strzelczyk, G.D.Bujacz, P.Kiełbasiński, J.Błaszczyk.

ABSTRACT

During crystallization screenings of commercially available hydrolytic enzymes, the new, hexagonal crystal form of CAL-B, has been discovered and hereby reported. The NAG molecules, which were closing the glycosylation site in the orthorhombic form, in hexagonal structure make the glycosylation site open. It is unknown whether the opening and closing of the glycosylation site by the 'lid' NAG molecules, could be related to the opening and closing of the active center of the enzyme upon substrate binding and product release.