PDBsum entry 2pc8

Hydrolase

PDB id: 2pc8

Contents

Protein chain

394 a.a. *

Ligands

BGC ×2

Waters ×288

* Residue conservation analysis

PDB id:

2pc8

Name:

Hydrolase

Title:

E292q mutant of exo-b-(1,3)-glucanase from candida albicans in complex with two separately bound glucopyranoside units at 1.8 a

Structure:

Hypothetical protein xog1. Chain: a. Engineered: yes. Mutation: yes

Source:

Candida albicans. Organism_taxid: 5476. Strain: atcc 10261. Gene: xog1. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.

Resolution:

1.80Å R-factor: 0.137 R-free: 0.163

Authors:

S.M.Cutfield,J.F.Cutfield,W.M.Patrick

Key ref:

W.M.Patrick et al. (2010). Carbohydrate binding sites in Candida albicans exo-β-1,3-glucanase and the role of the Phe-Phe 'clamp' at the active site entrance. Febs J, 277, 4549-4561. PubMed id: 20875088

Date:

29-Mar-07 Release date: 01-Apr-08

Protein chain

P29717  (EXG1_CANAL) -  Glucan 1,3-beta-glucosidase from Candida albicans (strain SC5314 / ATCC MYA-2876)

Seq: 438 a.a.

Struc: 394 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: E.C.2.4.1.- - ?????
• Enzyme class 2: E.C.3.2.1.58 - glucan 1,3-beta-glucosidase.
• Reaction: Successive hydrolysis of beta-D-glucose units from the non-reducing ends of 1,3-beta-D-glucans, releasing alpha-glucose.

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Febs J 277:4549-4561 (2010)

PubMed id: 20875088

Carbohydrate binding sites in Candida albicans exo-β-1,3-glucanase and the role of the Phe-Phe 'clamp' at the active site entrance.

W.M.Patrick, Y.Nakatani, S.M.Cutfield, M.L.Sharpe, R.J.Ramsay, J.F.Cutfield.

ABSTRACT

No abstract given.