PDBsum entry 2x8s

Hydrolase

PDB id

2x8s

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Contents

			Protein chains

					443 a.a.

			Ligands

					AHR-AHR-AHR ×2


					GOL ×6


					TRS


					PO4


					MPD

			Metals

					_CL ×3


					_CA


					_NA ×2

			Waters ×691

PDB id:

2x8s

Links

Name:

Hydrolase

Title:

Crystal structure of the abn2 d171a mutant in complex with arabinotriose

Structure:

Endo-alpha-1,5-l-arabinanase. Chain: a, b. Synonym: endo-alpha- arabinanase. Engineered: yes. Mutation: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.50Å

R-factor:

0.148

R-free:

0.167

Authors:

D.Desanctis,J.M.Inacio,P.F.Lindley,I.De Sa-Nogueira,I.Bento

Key ref:

D.de Sanctis et al. (2010). New evidence for the role of calcium in the glycosidase reaction of GH43 arabinanases. Febs J, 277, 4562-4574. PubMed id: 20883454

Date:

11-Mar-10

Release date:

23-Mar-11

PROCHECK

	Headers

	References

Protein chains

P42293 (EABN2_BACSU) - Extracellular endo-alpha-(1->5)-L-arabinanase 2 from Bacillus subtilis (strain 168)

Seq: Struc:					469 a.a. 443 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.3.2.1.99 - arabinan endo-1,5-alpha-L-arabinosidase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Endohydrolysis of 1,5-alpha-L-arabinofuranosidic linkages in 1,5-arabinans.

	Febs J 277:4562-4574 (2010)
PubMed id: 20883454

New evidence for the role of calcium in the glycosidase reaction of GH43 arabinanases.
D.de Sanctis, J.M.Inácio, P.F.Lindley, I.de Sá-Nogueira, I.Bento.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21426903

L.C.Tsai, C.H.Hsiao, W.Y.Liu, L.M.Yin, and L.F.Shyur (2011).
Structural basis for the inhibition of 1,3-1,4-β-D-glucanase by noncompetitive calcium ion and competitive Tris inhibitors.

Biochem Biophys Res Commun, 407, 593-598.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.