PDBsum entry 3oea

Hydrolase

PDB id: 3oea

Contents

Protein chains

146 a.a. *

Ligands

GLC-BGC-BGC-BGC-BGC ×2

Metals

_CA ×2

Waters ×497

* Residue conservation analysis

PDB id:

3oea

Name:

Hydrolase

Title:

Crystal structure of the q121e mutants of c.Polysaccharolyticus cbm16- 1 bound to cellopentaose

Structure:

S-layer associated multidomain endoglucanase. Chain: a, b. Fragment: unp residues 614-756. Engineered: yes. Mutation: yes

Source:

Caldanaerobius polysaccharolyticus. Organism_taxid: 44256. Gene: cela. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.35Å R-factor: 0.176 R-free: 0.204

Authors:

V.Agarwal,S.K.Nair

Key ref:

X.Su et al. (2010). Mutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules. J Biol Chem, 285, 34665-34676. PubMed id: 20739280

Date:

12-Aug-10 Release date: 25-Aug-10

Protein chains

Q9ZA17  (Q9ZA17_9THEO) -  S-layer associated multidomain endoglucanase from Caldanaerobius polysaccharolyticus

Seq: 1097 a.a.

Struc: 146 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

J Biol Chem 285:34665-34676 (2010)

PubMed id: 20739280

Mutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules.

X.Su, V.Agarwal, D.Dodd, B.Bae, R.I.Mackie, S.K.Nair, I.K.Cann.

ABSTRACT

No abstract given.