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Manganese in PDB 8bqr: Hen Egg-White Lysozyme (Hewl) Complexed with Biotin-Functionalised Anderson-Evans Polyoxometalate

Enzymatic activity of Hen Egg-White Lysozyme (Hewl) Complexed with Biotin-Functionalised Anderson-Evans Polyoxometalate

All present enzymatic activity of Hen Egg-White Lysozyme (Hewl) Complexed with Biotin-Functionalised Anderson-Evans Polyoxometalate:
3.2.1.17;

Protein crystallography data

The structure of Hen Egg-White Lysozyme (Hewl) Complexed with Biotin-Functionalised Anderson-Evans Polyoxometalate, PDB code: 8bqr was solved by S.Lentink, D.E.Salazar Marcano, M.A.Moussawi, L.Vandebroek, L.Vanmeervelt, T.N.Parac-Vogt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.70 / 2.32
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.394, 79.394, 35.136, 90, 90, 90
R / Rfree (%) 25.1 / 27.8

Other elements in 8bqr:

The structure of Hen Egg-White Lysozyme (Hewl) Complexed with Biotin-Functionalised Anderson-Evans Polyoxometalate also contains other interesting chemical elements:

Molybdenum (Mo) 6 atoms
Calcium (Ca) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Hen Egg-White Lysozyme (Hewl) Complexed with Biotin-Functionalised Anderson-Evans Polyoxometalate (pdb code 8bqr). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Hen Egg-White Lysozyme (Hewl) Complexed with Biotin-Functionalised Anderson-Evans Polyoxometalate, PDB code: 8bqr:

Manganese binding site 1 out of 1 in 8bqr

Go back to Manganese Binding Sites List in 8bqr
Manganese binding site 1 out of 1 in the Hen Egg-White Lysozyme (Hewl) Complexed with Biotin-Functionalised Anderson-Evans Polyoxometalate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Hen Egg-White Lysozyme (Hewl) Complexed with Biotin-Functionalised Anderson-Evans Polyoxometalate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:47.6
occ:0.44
 MN1 A:R9H201 0.0 47.6 0.4
O1 A:R9H201 1.9 58.4 0.4
O3 A:R9H201 1.9 57.2 0.4
O16 A:R9H201 1.9 55.9 0.4
O15 A:R9H201 1.9 60.8 0.4
O2 A:R9H201 2.0 59.7 0.4
O4 A:R9H201 2.0 56.0 0.4
C2 A:R9H201 2.9 59.0 0.4
C4 A:R9H201 2.9 59.3 0.4
C7 A:R9H201 2.9 58.5 0.4
C8 A:R9H201 3.0 57.0 0.4
C6 A:R9H201 3.0 58.7 0.4
C3 A:R9H201 3.0 56.2 0.4
C1 A:R9H201 3.0 58.0 0.4
C5 A:R9H201 3.0 58.7 0.4
O10 A:R9H201 3.3 57.6 0.4
O8 A:R9H201 3.3 54.6 0.4
O6 A:R9H201 3.3 54.2 0.4
O18 A:R9H201 3.3 54.8 0.4
MO6 A:R9H201 3.3 54.4 0.4
MO2 A:R9H201 3.3 56.4 0.4
MO4 A:R9H201 3.3 51.5 0.4
O20 A:R9H201 3.3 57.7 0.4
MO1 A:R9H201 3.3 51.1 0.4
MO3 A:R9H201 3.3 55.8 0.4
MO5 A:R9H201 3.3 54.4 0.4
O9 A:R9H201 3.3 56.2 0.4
N2 A:R9H201 4.4 61.4 0.4
O13 A:R9H201 4.5 50.3 0.4
O12 A:R9H201 4.5 53.2 0.4
N1 A:R9H201 4.5 60.8 0.4
O24 A:R9H201 4.5 53.2 0.4
O22 A:R9H201 4.5 61.4 0.4
O14 A:R9H201 4.5 54.7 0.4
O21 A:R9H201 4.5 55.5 0.4
O23 A:R9H201 4.5 57.9 0.4
O11 A:R9H201 4.5 53.5 0.4
O7 A:R9H201 4.6 56.2 0.4
O17 A:R9H201 4.6 49.6 0.4
O5 A:R9H201 4.6 57.1 0.4
O19 A:R9H201 4.6 58.2 0.4

Reference:

S.Lentink, D.Salazar Marcano, M.A.Moussawi, L.Vandebroek, L.Van Meervelt, T.Parac-Vogt. Fine-Tuning Non-Covalent Interactions Between Hybrid Metal-Oxo Clusters and Proteins Faraday Disc.Chem.Soc 2022.
ISSN: ESSN 1364-5498
DOI: 10.1039/D2FD00161F
Page generated: Sun Oct 6 11:26:50 2024

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