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Terbium in PDB 8piw: Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4-NMET2

Enzymatic activity of Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4-NMET2

All present enzymatic activity of Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4-NMET2:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4-NMET2, PDB code: 8piw 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) 38.76 / 1.72
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.521, 77.521, 37.793, 90, 90, 90
R / Rfree (%) 17.2 / 19.6

Other elements in 8piw:

The structure of Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4-NMET2 also contains other interesting chemical elements:

Sodium (Na) 1 atom
Chlorine (Cl) 6 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-NMET2 (pdb code 8piw). 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-NMET2, PDB code: 8piw:

Terbium binding site 1 out of 1 in 8piw

Go back to Terbium Binding Sites List in 8piw
Terbium binding site 1 out of 1 in the Crystal Structure of Hen Egg White Lysozyme Co-Crystallized with 10 Mm TBXO4-NMET2


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-NMET2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Tb201

b:39.7
occ:0.55
 H91 A:ZHT202 1.8 41.7 0.6
N5 A:ZHT202 2.3 31.6 0.6
OD2 A:ASP101 2.3 32.5 1.0
O3 A:ZHT202 2.4 30.2 0.6
O1 A:ZHT202 2.4 29.3 0.6
OD1 A:ASP101 2.5 38.6 1.0
CG A:ASP101 2.7 36.0 1.0
H82 A:ZHT202 2.7 40.5 0.6
C9 A:ZHT202 2.7 34.8 0.6
N4 A:ZHT202 2.7 31.1 0.6
N1 A:ZHT202 2.8 35.9 0.6
N2 A:ZHT202 2.8 34.0 0.6
H181 A:ZHT202 3.1 40.0 0.6
C19 A:ZHT202 3.1 32.5 0.6
C23 A:ZHT202 3.1 31.2 0.6
C24 A:ZHT202 3.2 30.5 0.6
C18 A:ZHT202 3.2 33.3 0.6
H42 A:ZHT202 3.2 43.6 0.6
H41 A:ZHT202 3.3 43.6 0.6
C8 A:ZHT202 3.3 33.7 0.6
C4 A:ZHT202 3.3 36.4 0.6
N3 A:ZHT202 3.3 34.0 0.6
H92 A:ZHT202 3.3 41.7 0.6
C17 A:ZHT202 3.3 29.7 0.6
C10 A:ZHT202 3.4 35.5 0.6
C16 A:ZHT202 3.5 30.4 0.6
C12 A:ZHT202 3.6 31.9 0.6
H112 A:ZHT202 3.7 39.5 0.6
C7 A:ZHT202 3.7 34.0 0.6
C5 A:ZHT202 3.7 35.5 0.6
C11 A:ZHT202 3.7 32.9 0.6
C6 A:ZHT202 3.8 34.9 0.6
H52 A:ZHT202 3.8 42.6 0.6
H102 A:ZHT202 4.0 42.6 0.6
H101 A:ZHT202 4.1 42.6 0.6
H182 A:ZHT202 4.2 40.0 0.6
H72 A:ZHT202 4.2 40.8 0.6
H81 A:ZHT202 4.2 40.5 0.6
CB A:ASP101 4.2 30.3 1.0
H A:GLY102 4.2 46.4 1.0
H61 A:ZHT202 4.3 42.0 0.6
O2 A:ZHT202 4.4 30.2 0.6
H71 A:ZHT202 4.4 40.8 0.6
O A:HOH305 4.4 43.1 1.0
C20 A:ZHT202 4.5 32.0 0.6
C22 A:ZHT202 4.5 31.4 0.6
O A:ZHT202 4.5 29.4 0.6
H51 A:ZHT202 4.6 42.6 0.6
HB3 A:ASP101 4.6 36.4 1.0
H62 A:ZHT202 4.6 42.0 0.6
HB2 A:ASP101 4.6 36.4 1.0
H111 A:ZHT202 4.7 39.5 0.6
HA A:ASP101 4.8 32.3 1.0
C3 A:ZHT202 4.8 36.8 0.6
C15 A:ZHT202 4.9 30.9 0.6
C13 A:ZHT202 5.0 31.4 0.6

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 00900 2024.
ISSN: ISSN 0947-6539
PubMed: 38738452
DOI: 10.1002/CHEM.202400900
Page generated: Fri Oct 11 08:55:38 2024

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