PDBsum entry 3o2l

Hydrolase

PDB id: 3o2l

Contents

Protein chain

306 a.a.

Waters ×204

PDB id:

3o2l

Name:

Hydrolase

Title:

Crystal structure of an inactive kemp elimination design hg-1

Structure:

Endo-1,4-beta-xylanase. Chain: a. Fragment: unp residues 27-329. Synonym: xylanase, 1,4-beta-d-xylan xylanohydrolase, taxi. Engineered: yes. Mutation: yes

Source:

Thermoascus aurantiacus. Organism_taxid: 5087. Gene: xyna. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.170 R-free: 0.229

Authors:

L.M.Thomas,H.K.Privett,S.L.Mayo

Key ref:

H.K.Privett et al. (2012). Iterative approach to computational enzyme design. Proc Natl Acad Sci U S A, 109, 3790-3795. PubMed id: 22357762

Date:

22-Jul-10 Release date: 20-Jul-11

Protein chain

P23360  (XYNA_THEAU) -  Endo-1,4-beta-xylanase from Thermoascus aurantiacus

Seq: 329 a.a.

Struc: 306 a.a.*

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.2.1.8 - endo-1,4-beta-xylanase.
• Reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.

Proc Natl Acad Sci U S A 109:3790-3795 (2012)

PubMed id: 22357762

Iterative approach to computational enzyme design.

H.K.Privett, G.Kiss, T.M.Lee, R.Blomberg, R.A.Chica, L.M.Thomas, D.Hilvert, K.N.Houk, S.L.Mayo.

ABSTRACT

No abstract given.