Structure analysis

PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES

X-ray diffraction
1.9Å resolution
Source organism: Escherichia virus T4
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 8653.13 Å2
Buried surface area: 215.21 Å2
Dissociation area: 107.6 Å2
Dissociation energy (ΔGdiss): 2.75 kcal/mol
Dissociation entropy (TΔSdiss): 0.14 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133020
    Assembly 1
Confidence : 95%
No. subunits : 1
Symmetry : None
3DComplex & QSbio predictionx
No. subunits : 1
Symmetry : None
Evidence : This biological assembly agrees with the prediction of both PISA & EPPIC

Macromolecules

Chain: A
Length: 164 amino acids
Theoretical weight: 18.61 KDa
Source organism: Escherichia virus T4
Expression system: Not provided
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Pfam: Phage lysozyme
InterPro:
CATH: Lysozyme
SCOP: Phage lysozyme
PDBe-KB: UniProt Coverage View: P00720  
116420406080100120140160
 
50100150
UniProt
P00720
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites

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