PDBsum entry: 1ups

Glycosyl hydrolase

PDB-id: 1ups

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

402 a.a. *

Metal ions

_CA ×2

Waters ×378

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

1ups

Name:

Glycosyl hydrolase

Title:

Glcnac[alpha]1-4gal releasing endo-[beta]-galactosidase from clostridium perfringens

Structure:

Glcnac-alpha-1,4-gal-releasing endo-beta- galactosidase. Chain: a, b. Engineered: yes

Source:

Clostridium perfringens. Organism_taxid: 1502. Atcc: 10543. Expressed in: escherichia coli. Expression_system_taxid: 562

UniProt:

Chains A, B: Q934G8 (Q934G8_CLOPE)

Seq:

Struc:

Seq:

420 a.a.

Struc:

402 a.a.

Key:	PfamA domain	PfamB domain
Secondary structure	CATH domain

Resolution:

1.82Å

R-factor:

0.177

R-free:

0.204

Authors:

W.Tempel,Z.-J.Liu,P.S.Horanyi,L.Deng,D.Lee,M.G.Newton, J.P.Rose,H.Ashida,S.-C.Li,Y.-T.Li,B.-C.Wang, Southeast Collaboratory For Structural Genomics (Secsg)

Key ref:

W.Tempel et al. (2005). Three-dimensional structure of GlcNAcalpha1-4Gal releasing endo-beta-galactosidase from Clostridium perfringens.. Proteins, 59, 141-144. [PubMed id: 15688452] [DOI: 10.1002/prot.20363]

Date:

10-Oct-03

Release date:

25-Nov-04

Related entries:

Cpe-ebgal related db: targetdb

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1002/prot.20363

Proteins 59:141-144 (2005)

PubMed id: 15688452

Three-dimensional structure of GlcNAcalpha1-4Gal releasing endo-beta-galactosidase from Clostridium perfringens.

W.Tempel, Z.J.Liu, P.S.Horanyi, L.Deng, D.Lee, M.G.Newton, J.P.Rose, H.Ashida, S.C.Li, Y.T.Li, B.C.Wang.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Stereographic cartoon of the Endo- -Gal[GnGa] molecule. The partially disordered loop connecting the 2 globular domains is represented as a dashed line.

Figure 2.
Figure 2. The -strand topology of Endo- -Gal[GNGa]. The larger N-terminal domain consists of a -sheet sandwich. The smaller C-terminal domain is an assembly of 6 double-stranded sheets. For clarity, the length of strand symbols and linkers do not represent their relative sizes in the peptide. Coloring roughly corresponds to that in Figure 1.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 59, 141-144) copyright 2005.

Figures were selected by an automated process.