Atomistry » Calcium » PDB 5lia-5m27 » 5lul
Atomistry »
  Calcium »
    PDB 5lia-5m27 »
      5lul »

Calcium in PDB 5lul: Structure of A Triple Variant of Cutinase 2 From Thermobifida Cellulosilytica

Protein crystallography data

The structure of Structure of A Triple Variant of Cutinase 2 From Thermobifida Cellulosilytica, PDB code: 5lul was solved by A.Hromic, A.Lyskowski, K.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.53 / 1.90
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 110.438, 110.438, 75.302, 90.00, 90.00, 120.00
R / Rfree (%) 15.9 / 19.4

Other elements in 5lul:

The structure of Structure of A Triple Variant of Cutinase 2 From Thermobifida Cellulosilytica also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of A Triple Variant of Cutinase 2 From Thermobifida Cellulosilytica (pdb code 5lul). 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 Structure of A Triple Variant of Cutinase 2 From Thermobifida Cellulosilytica, PDB code: 5lul:

Calcium binding site 1 out of 1 in 5lul

Go back to Calcium Binding Sites List in 5lul
Calcium binding site 1 out of 1 in the Structure of A Triple Variant of Cutinase 2 From Thermobifida Cellulosilytica


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of A Triple Variant of Cutinase 2 From Thermobifida Cellulosilytica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:40.6
occ:1.00
O A:ALA35 2.3 21.8 1.0
O A:ARG32 2.5 23.9 1.0
O A:HOH568 2.5 33.4 1.0
O A:PHE38 2.6 19.5 1.0
O A:HOH541 2.7 24.6 1.0
O A:HOH503 2.9 30.1 1.0
C A:ALA35 3.5 21.5 1.0
C A:ARG32 3.7 24.0 1.0
C A:PHE38 3.8 20.7 1.0
CB A:ALA35 4.2 20.4 1.0
CA A:ALA35 4.2 20.9 1.0
O A:HOH489 4.2 25.9 1.0
OD1 A:ASN88 4.3 22.2 1.0
N A:ALA35 4.3 21.0 1.0
CG A:ARG32 4.3 22.2 0.5
N A:PHE38 4.3 15.5 1.0
CG A:ARG32 4.4 22.3 0.5
CA A:ARG32 4.4 20.2 0.5
CA A:ARG32 4.5 20.2 0.5
CA A:GLY39 4.5 15.4 1.0
N A:ASP36 4.6 22.5 1.0
N A:GLY39 4.6 14.5 1.0
N A:GLY37 4.6 21.4 1.0
N A:PHE33 4.6 21.3 1.0
CA A:PHE33 4.7 23.4 1.0
O A:PHE33 4.7 22.4 1.0
CA A:PHE38 4.7 17.3 1.0
CA A:ASP36 4.7 26.9 1.0
C A:PHE33 4.8 22.2 1.0
C A:GLY39 4.9 15.3 1.0

Reference:

D.Ribitsch, A.Hromic, S.Zitzenbacher, B.Zartl, C.Gamerith, A.Pellis, A.Jungbauer, A.Yskowski, G.Steinkellner, K.Gruber, R.Tscheliessnig, E.Herrero Acero, G.M.Guebitz. Small Cause, Large Effect: Structural Characterization of Cutinases From Thermobifida Cellulosilytica. Biotechnol. Bioeng. V. 114 2481 2017.
ISSN: ESSN 1097-0290
PubMed: 28671263
DOI: 10.1002/BIT.26372
Page generated: Mon Jul 15 07:48:20 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