Atomistry » Calcium » PDB 8ihn-8izi » 8ihy
Atomistry »
  Calcium »
    PDB 8ihn-8izi »
      8ihy »

Calcium in PDB 8ihy: X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida

Protein crystallography data

The structure of X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida, PDB code: 8ihy 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) 40.29 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.36, 71.639, 55.184, 90, 114.04, 90
R / Rfree (%) 14.7 / 17.7

Other elements in 8ihy:

The structure of X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the X-Ray Crystal Structure of Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida (pdb code 8ihy). 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 Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida, PDB code: 8ihy:

Calcium binding site 1 out of 1 in 8ihy

Go back to Calcium Binding Sites List in 8ihy
Calcium binding site 1 out of 1 in the X-Ray Crystal Structure of Q387E 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 Q387E Mutant of Endo-1,4-Beta Glucanase From Eisenia Fetida within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:9.2
occ:1.00
O A:HOH670 2.3 7.3 1.0
O A:HOH888 2.4 9.1 1.0
O A:ALA230 2.4 8.5 1.0
O A:ASN271 2.4 9.8 1.0
OD1 A:ASP233 2.5 8.9 1.0
OE1 A:GLU234 2.5 7.6 1.0
OE2 A:GLU234 2.6 7.8 1.0
OD2 A:ASP233 2.6 9.0 1.0
CG A:ASP233 2.9 8.2 1.0
CD A:GLU234 2.9 8.3 1.0
C A:ALA230 3.6 6.8 1.0
C A:ASN271 3.7 9.8 1.0
OD1 A:ASN271 4.2 9.4 1.0
N A:ALA230 4.3 8.5 1.0
CB A:ASP233 4.4 8.4 1.0
CG A:GLU234 4.4 5.1 1.0
CA A:ALA230 4.4 9.4 1.0
OG A:SER228 4.5 7.2 1.0
N A:TYR231 4.5 7.0 1.0
N A:GLU272 4.5 7.8 1.0
CA A:TYR231 4.5 7.8 1.0
CA A:ASN271 4.6 7.6 1.0
N A:GLU234 4.6 7.7 1.0
CA A:GLU272 4.6 7.4 1.0
CG A:ASN271 4.6 11.1 1.0
CB A:ALA230 4.7 11.6 1.0
CZ A:PHE83 4.9 8.0 1.0
N A:ASP233 4.9 6.6 1.0
OG A:SER229 4.9 13.2 1.0
O A:HOH908 4.9 19.0 1.0
N A:LYS273 5.0 8.0 1.0
C A:TYR231 5.0 7.4 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 09:39:43 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy