PDBsum entry 4gcc

Hydrolase

PDB id: 4gcc

Contents

Protein chain

129 a.a.

Ligands

DMS ×4

CPT ×2

Waters ×44

PDB id:

4gcc

Name:

Hydrolase

Title:

Room temperature x-ray diffraction study of a 6-fold molar excess of a cisplatin/carboplatin mixture binding to hewl, dataset 1

Structure:

LysozymE C. Chain: a. Fragment: unp residues 19-147. Synonym: 1,4-beta-n-acetylmuramidasE C, allergen gal d iv. Ec: 3.2.1.17

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Tissue: egg white

Resolution:

2.00Å R-factor: 0.189 R-free: 0.248

Authors:

J.R.Helliwell,S.W.M.Tanley

Key ref:

J.R.Helliwell and S.W.Tanley (2013). The crystal structure analysis of the relative binding of cisplatin and carboplatin in a mixture with histidine in a protein studied at 100 and 300 K with repeated X-ray irradiation. Acta Crystallogr D Biol Crystallogr, 69, 121-125. PubMed id: 23275170

Date:

30-Jul-12 Release date: 02-Jan-13

Protein chain

P00698  (LYSC_CHICK) -  Lysozyme C from Gallus gallus

Seq: 147 a.a.

Struc: 129 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.17 - lysozyme.
• Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

Acta Crystallogr D Biol Crystallogr 69:121-125 (2013)

PubMed id: 23275170

The crystal structure analysis of the relative binding of cisplatin and carboplatin in a mixture with histidine in a protein studied at 100 and 300 K with repeated X-ray irradiation.

J.R.Helliwell, S.W.Tanley.

ABSTRACT

No abstract given.