PDBsum entry: 1jwq

Hydrolase

PDB id: 1jwq

Contents

Protein chain

179 a.a. *

Metals

_ZN

Waters ×229

* Residue conservation analysis

PDB id:

1jwq

Name:

Hydrolase

Title:

Structure of the catalytic domain of cwlv, n-acetylmuramoyl- l-alanine amidase from bacillus(paenibacillus) polymyxa var.Colistinus

Structure:

N-acetylmuramoyl-l-alanine amidase cwlv. Chain: a. Fragment: catalytic domain. Engineered: yes

Source:

Paenibacillus polymyxa. Organism_taxid: 1406. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.80Å R-factor: 0.176 R-free: 0.206

Authors:

T.Yamane,Y.Koyama,Y.Nojiri,T.Hikage,M.Akita,A.Suzuki, T.Shirai,F.Ise,T.Shida,J.Sekiguchi

Key ref:

T.Yamane et al. The structure of the catalytic domain of n-Acetylmuramoyl-L-Alanine amidase, A cell wall hydrolase from bacillus polymyxa var.Colistinus and its resemblance to the structure of carboxypeptidases. To be published,

Date:

05-Sep-01 Release date: 18-Nov-03

Protein chain

Q9LCR3  (Q9LCR3_PAEPO) -  CwlV

Seq: 499 a.a.

Struc: 179 a.a.*

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

 Gene Ontology (GO) functional annotation 

• Biological process: peptidoglycan catabolic process (1 term)
• Biochemical function: N-acetylmuramoyl-L-alanine amidase activity (1 term)