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Calcium in PDB 8ihw: X-Ray Crystal Structure of D43R Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida

Protein crystallography data

The structure of X-Ray Crystal Structure of D43R Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida, PDB code: 8ihw was solved by C.Kuroki, Y.Hirano, M.Nakazawa, T.Sakamoto, T.Tamada, M.Ueda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.60 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.292, 71.682, 55.359, 90, 114.23, 90
R / Rfree (%) 14.4 / 17.6

Other elements in 8ihw:

The structure of X-Ray Crystal Structure of D43R Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the X-Ray Crystal Structure of D43R Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida (pdb code 8ihw). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the X-Ray Crystal Structure of D43R Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida, PDB code: 8ihw:

Calcium binding site 1 out of 1 in 8ihw

Go back to Calcium Binding Sites List in 8ihw
Calcium binding site 1 out of 1 in the X-Ray Crystal Structure of D43R Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of X-Ray Crystal Structure of D43R Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca503

b:4.7
occ:1.00
O A:HOH665 2.4 4.2 1.0
O A:HOH914 2.4 5.0 1.0
O A:ASN271 2.4 4.9 1.0
OE1 A:GLU234 2.4 2.8 1.0
OD1 A:ASP233 2.4 5.1 1.0
O A:ALA230 2.4 3.2 1.0
OE2 A:GLU234 2.5 2.8 1.0
OD2 A:ASP233 2.5 4.8 1.0
CD A:GLU234 2.8 5.0 1.0
CG A:ASP233 2.8 3.1 1.0
C A:ALA230 3.6 3.2 1.0
C A:ASN271 3.6 3.3 1.0
OD1 A:ASN271 4.2 4.4 1.0
O A:HOH1014 4.3 26.3 1.0
N A:ALA230 4.3 4.8 1.0
CG A:GLU234 4.3 2.9 1.0
CB A:ASP233 4.3 2.4 1.0
CA A:ALA230 4.4 4.6 1.0
OG A:SER228 4.5 2.9 1.0
N A:GLU272 4.5 2.4 1.0
N A:TYR231 4.5 2.8 1.0
CA A:ASN271 4.5 3.8 1.0
CA A:TYR231 4.5 3.9 1.0
N A:GLU234 4.6 2.4 1.0
CA A:GLU272 4.6 1.6 1.0
CG A:ASN271 4.6 4.8 1.0
CB A:ALA230 4.8 4.1 1.0
N A:ASP233 4.9 4.3 1.0
N A:LYS273 4.9 2.7 1.0
CZ A:PHE83 4.9 3.7 1.0
O A:HOH961 4.9 12.7 1.0
OG A:SER229 5.0 8.1 1.0
NZ A:LYS273 5.0 2.2 1.0
C A:TYR231 5.0 2.9 1.0

Reference:

C.Kuroki, Y.Hirano, M.Nakazawa, T.Sakamoto, T.Tamada, M.Ueda. A Single Mutation ASP43ARG Was Increased 2.5-Fold the Catalytic Activity and Maintained the Stability of Cold-Adapted Endo-1,4-Beta Glucanase (Ef-EG2) From Eisenia Fetida. Curr Res Biotechnol V. 5 2023.
DOI: 10.1016/J.CRBIOT.2023.100126
Page generated: Fri Jul 19 09:39:16 2024

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