PDBsum entry: 2dsk

Hydrolase

PDB-id: 2dsk

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

300 a.a. *

Ligands

GOL ×6

SO4

Waters ×650

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

2dsk

Name:

Hydrolase

Title:

Crystal structure of catalytic domain of hyperthermophilic chitinase from pyrococcus furiosus

Structure:

Chitinase. Chain: a, b. Fragment: catalutic domain (ad2). Engineered: yes

Source:

Pyrococcus furiosus. Organism_taxid: 2261. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:

Chains A, B: Q8U1H5 (Q8U1H5_PYRFU)

Seq:

Struc:

Seq:

Struc:

Seq:

717 a.a.

Struc:

300 a.a.*

Key:

PfamA domain

Secondary structure

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

Resolution:

1.50Å

R-factor:

0.168

R-free:

0.180

Authors:

T.Nakamura,S.Mine,Y.Hagihara,K.Ishikawa,K.Uegaki

Key ref:

T.Nakamura et al. (2007). Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus.. Acta Crystallograph Sect F Struct Biol Cryst Commun, 63, 7. [PubMed id: 17183162]

Date:

30-Jun-06

Release date:

06-Feb-07

Quick_links

Procheck

Clefts

Surface

Key reference

Full text	Acta Crystallograph Sect F Struct Biol Cryst Commun 63:7 (2007)
PubMed id: 17183162

Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus.

T.Nakamura, S.Mine, Y.Hagihara, K.Ishikawa, K.Uegaki.

ABSTRACT

The crystal structure of the catalytic domain of a chitinase from the hyperthermophilic archaeon Pyrococcus furiosus (AD2(PF-ChiA)) has been determined at 1.5 A resolution. This is the first structure of the catalytic domain of an archaeal chitinase. The overall structure of AD2(PF-ChiA) is a TIM-barrel fold with a tunnel-like active site that is a common feature of family 18 chitinases. Although the catalytic residues (Asp522, Asp524 and Glu526) are conserved, comparison of the conserved residues and structures with those of other homologous chitinases indicates that the catalytic mechanism of PF-ChiA is different from that of family 18 chitinases.