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Magnesium in PDB 4zu3: Halohydrin Hydrogen-Halide-Lyases, Hheb

Protein crystallography data

The structure of Halohydrin Hydrogen-Halide-Lyases, Hheb, PDB code: 4zu3 was solved by F.Watanabe, F.Yu, A.Ohtaki, Y.Yamanaka, K.Noguchi, M.Yohda, M.Odaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.01 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 122.910, 215.640, 104.721, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 20.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Halohydrin Hydrogen-Halide-Lyases, Hheb (pdb code 4zu3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Halohydrin Hydrogen-Halide-Lyases, Hheb, PDB code: 4zu3:

Magnesium binding site 1 out of 1 in 4zu3

Go back to Magnesium Binding Sites List in 4zu3
Magnesium binding site 1 out of 1 in the Halohydrin Hydrogen-Halide-Lyases, Hheb


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Halohydrin Hydrogen-Halide-Lyases, Hheb within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg302

b:27.5
occ:0.91
O E:ARG54 2.3 29.7 1.0
O E:HOH456 2.3 23.6 1.0
O E:HOH413 2.7 23.4 1.0
C E:ARG54 3.4 25.4 1.0
HA E:ARG54 3.7 36.9 1.0
HG3 E:ARG54 4.0 48.9 1.0
CA E:ARG54 4.1 30.8 1.0
C E:ALA55 4.4 27.6 1.0
N E:ALA55 4.5 23.7 1.0
HA E:ALA55 4.5 35.0 1.0
O E:HOH483 4.5 29.3 1.0
HG2 E:ARG54 4.5 48.9 1.0
O E:ALA55 4.6 22.9 1.0
HA3 E:GLY56 4.6 42.7 1.0
O E:GLU53 4.6 25.6 1.0
O E:HOH495 4.6 32.8 1.0
N E:GLY56 4.6 32.1 1.0
CG E:ARG54 4.6 40.8 1.0
O E:HOH559 4.7 21.5 1.0
CA E:ALA55 4.7 29.2 1.0
H E:GLY56 4.8 38.5 1.0
CB E:ARG54 5.0 25.9 1.0

Reference:

F.Watanabe, F.Yu, A.Ohtaki, Y.Yamanaka, K.Noguchi, M.Yohda, M.Odaka. Crystal Structures of Halohydrin Hydrogen-Halide-Lyases From Corynebacterium Sp. N-1074 Proteins V. 83 2230 2015.
ISSN: ESSN 1097-0134
PubMed: 26422370
DOI: 10.1002/PROT.24938
Page generated: Mon Dec 14 19:58:31 2020

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