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Krypton in PDB 1c6q: T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Krypton

Enzymatic activity of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Krypton

All present enzymatic activity of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Krypton:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Krypton, PDB code: 1c6q was solved by M.L.Quillin, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.010, 61.010, 97.276, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1c6q:

The structure of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Krypton also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Krypton Binding Sites:

The binding sites of Krypton atom in the T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Krypton (pdb code 1c6q). This binding sites where shown within 5.0 Angstroms radius around Krypton atom.
In total only one binding site of Krypton was determined in the T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Krypton, PDB code: 1c6q:

Krypton binding site 1 out of 1 in 1c6q

Go back to Krypton Binding Sites List in 1c6q
Krypton binding site 1 out of 1 in the T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Krypton


Mono view


Stereo pair view

A full contact list of Krypton with other atoms in the Kr binding site number 1 of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Krypton within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Kr500

b:15.3
occ:0.36
CD2 A:LEU118 3.5 16.9 1.0
SD A:MET102 3.8 18.2 1.0
CD2 A:LEU133 3.9 17.9 1.0
CD1 A:LEU121 4.0 18.1 1.0
CG1 A:VAL111 4.0 15.9 1.0
CB A:PHE114 4.0 18.6 1.0
CE A:MET102 4.1 15.7 1.0
CG A:LEU118 4.1 24.2 1.0
CD1 A:LEU99 4.2 14.8 1.0
CB A:SER117 4.2 17.9 1.0
CG A:PHE114 4.5 22.6 1.0
CD2 A:PHE114 4.5 27.1 1.0
N A:LEU118 4.6 13.4 1.0
O A:VAL111 4.7 18.4 1.0
CA A:LEU118 4.8 18.9 1.0
O A:PHE114 4.8 18.0 1.0
C A:SER117 4.9 14.4 1.0
CZ A:PHE153 4.9 13.9 1.0

Reference:

M.L.Quillin, W.A.Breyer, I.J.Griswold, B.W.Matthews. Size Versus Polarizability in Protein-Ligand Interactions: Binding of Noble Gases Within Engineered Cavities in Phage T4 Lysozyme. J.Mol.Biol. V. 302 955 2000.
ISSN: ISSN 0022-2836
PubMed: 10993735
DOI: 10.1006/JMBI.2000.4063
Page generated: Sun Jan 24 17:57:35 2021

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