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Terbium in PDB 8owc: Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4

Enzymatic activity of Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4

All present enzymatic activity of Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4, PDB code: 8owc was solved by Z.Alsalman, E.Girard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.75 / 1.70
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.474, 77.474, 37.491, 90, 90, 90
R / Rfree (%) 17.5 / 20.9

Other elements in 8owc:

The structure of Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4 also contains other interesting chemical elements:

Sodium (Na) 1 atom
Chlorine (Cl) 7 atoms

Terbium Binding Sites:

The binding sites of Terbium atom in the Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4 (pdb code 8owc). This binding sites where shown within 5.0 Angstroms radius around Terbium atom.
In total only one binding site of Terbium was determined in the Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4, PDB code: 8owc:

Terbium binding site 1 out of 1 in 8owc

Go back to Terbium Binding Sites List in 8owc
Terbium binding site 1 out of 1 in the Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4


Mono view


Stereo pair view

A full contact list of Terbium with other atoms in the Tb binding site number 1 of Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Tb201

b:53.4
occ:0.60
 OD2 A:ASP101 2.2 44.0 1.0
H061 A:7MT202 2.2 49.2 0.6
N23 A:7MT202 2.5 50.2 0.6
N02 A:7MT202 2.6 43.8 0.6
N17 A:7MT202 2.7 49.1 0.6
OD1 A:ASP101 2.7 87.0 1.0
CG A:ASP101 2.8 61.2 1.0
H301 A:7MT202 2.9 54.7 0.6
O25 A:7MT202 2.9 55.5 0.6
N09 A:7MT202 2.9 42.3 0.6
H012 A:7MT202 3.1 49.6 0.6
C30 A:7MT202 3.1 45.6 0.6
N06 A:7MT202 3.1 41.0 0.6
C01 A:7MT202 3.2 41.4 0.6
C22 A:7MT202 3.3 52.2 0.6
C10 A:7MT202 3.3 48.1 0.6
C24 A:7MT202 3.4 54.7 0.6
C11 A:7MT202 3.4 48.3 0.6
O28 A:7MT202 3.5 54.1 0.6
H051 A:7MT202 3.5 50.8 0.6
C05 A:7MT202 3.6 42.4 0.6
C03 A:7MT202 3.6 41.6 0.6
C29 A:7MT202 3.6 45.1 0.6
C04 A:7MT202 3.6 42.8 0.6
C16 A:7MT202 3.8 51.0 0.6
H291 A:7MT202 3.8 54.0 0.6
C08 A:7MT202 3.9 42.1 0.6
H302 A:7MT202 4.0 54.7 0.6
H081 A:7MT202 4.0 50.4 0.6
C07 A:7MT202 4.0 41.7 0.6
C18 A:7MT202 4.1 53.0 0.6
H011 A:7MT202 4.1 49.6 0.6
H042 A:7MT202 4.2 51.2 0.6
H032 A:7MT202 4.2 49.9 0.6
H041 A:7MT202 4.2 51.2 0.6
H031 A:7MT202 4.2 49.9 0.6
CB A:ASP101 4.3 34.8 1.0
H A:GLY102 4.4 67.0 1.0
H292 A:7MT202 4.5 54.0 0.6
O26 A:7MT202 4.5 56.4 0.6
H072 A:7MT202 4.5 50.0 0.6
H052 A:7MT202 4.5 50.8 0.6
HB2 A:ASP101 4.6 41.8 1.0
C21 A:7MT202 4.6 51.5 0.6
C19 A:7MT202 4.7 49.7 0.6
HB3 A:ASP101 4.7 41.8 1.0
C13 A:7MT202 4.7 49.1 0.6
H082 A:7MT202 4.7 50.4 0.6
O A:HOH319 4.7 51.6 1.0
H071 A:7MT202 4.8 50.0 0.6
HA A:ASP101 5.0 30.7 1.0

Reference:

A.Roux, Z.Alsalman, T.Jiang, J.C.Mulatier, D.Pitrat, E.Dumont, F.Riobe, N.Gillet, E.Girard, O.Maury. Influence of Chemical Modifications of the Crystallophore on Protein Nucleating Properties and Supramolecular Interactions Network. Chemistry V. 30 00900 2024.
ISSN: ISSN 0947-6539
PubMed: 38738452
DOI: 10.1002/CHEM.202400900
Page generated: Tue Aug 19 06:12:53 2025

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