PDBsum entry: 2drq

Hydrolase

PDB-id: 2drq

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

377 a.a. *

Ligands

GOL

Metal ions

_NI

Waters ×430

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

2drq

Name:

Hydrolase

Title:

Crystal structure of reducing-end-xylose releasing exo- oligoxylanase d263g mutant

Structure:

Xylanase y. Chain: a. Synonym: reducing-end-xylose releasing exo-oligoxylanase. Engineered: yes. Mutation: yes

Source:

Bacillus halodurans c-125. Organism_taxid: 272558. Strain: c-125. Gene: bh2105. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:

Q9KB30 (Q9KB30_BACHD)

Seq:

Struc:

Seq:

388 a.a.

Struc:

377 a.a.*

Key:	PfamA domain
Secondary structure	CATH domain

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

Resolution:

2.10Å

R-factor:

0.145

R-free:

0.194

Authors:

S.Fushinobu,M.Hidaka,Y.Honda,T.Wakagi,H.Shoun,M.Kitaoka

Key ref:

M.Hidaka et al. (2009). Structural explanation for the acquisition of glycosynthase activity.. J Biochem, 0, . [PubMed id: 19819900] [DOI: 10.1093/jb/mvp159]

Date:

12-Jun-06

Release date:

27-Jun-06

Related entries:

1wu4
the same protein (wild type).
1wu5
the same protein (wild type) complexed with xylose.
1wu6
the same protein (e70a) complexed with xylobiose.
2dro
the same protein (d263c)
2drr
the same protein (d263n)
... plus others (see Header records)

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1093/jb/mvp159

J Biochem 0: (2009)

PubMed id: 19819900

Structural explanation for the acquisition of glycosynthase activity.

M.Hidaka, S.Fushinobu, Y.Honda, T.Wakagi, H.Shoun, M.Kitaoka.

ABSTRACT

No abstract given.