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Ligands
Code Name Style Show Link
BME Beta-mercaptoethanol
CL Chloride ion
XE Xenon
Non-standard Residues
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Glycosylation
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Modification
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Code : 1C65   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : T4 LYSOZYME MUTANT C54T/C97A/L121A IN THE PRESENCE OF 8 ATM XENON
Release Data : 2000-10-04
Compound :
mol_id molecule chains
1 PROTEIN (LYSOZYME) A
ec: 3.2.1.17
mutation: YES
Source :
mol_id organism_scientific expression_system
1 Enterobacteria phage T4  (taxid:10665) Escherichia coli  (taxid:562)
gene: GENE E
expression_system_plasmid: PHS1403
Authors : Quillin, M.L., Matthews, B.W.
Keywords : HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme.

Quillin, M.L.,Breyer, W.A.,Griswold, I.J.  et al.
(2000)  J.Mol.Biol.  302 : 955 - 977

PubMed: 10993735
DOI: 10.1006/jmbi.2000.4063

Response of a Protein Structure to Cavity-Creating Mutations and its Relation to the Hydrophobic Effect

Eriksson, A.E.,Baase, W.A.,Zhang, X.-J.  et al.
(1992)  Science  255 : 178

Structure of Bacteriophage T4 Lysozyme Refined at 1.7 A Resolution

Weaver, L.H.,Matthews, B.W.
(1987)  J.Mol.Biol.  193 : 189

Chain : A
UniProt : P00720 (ENLYS_BPT4)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. 3.2.1.17 HAMAP-Rule:MF_04110, PubMed:4865643
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