Calcium in PDB 5dpn: Engineered Cbm X-2 L110F in Complex with Branched Carbohydrate Xxxg.

Protein crystallography data

The structure of Engineered Cbm X-2 L110F in Complex with Branched Carbohydrate Xxxg., PDB code: 5dpn was solved by M.Ohlin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 72.977, 49.856, 45.091, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 20.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Engineered Cbm X-2 L110F in Complex with Branched Carbohydrate Xxxg. (pdb code 5dpn). 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 Engineered Cbm X-2 L110F in Complex with Branched Carbohydrate Xxxg., PDB code: 5dpn:

Calcium binding site 1 out of 1 in 5dpn

Go back to Calcium Binding Sites List in 5dpn
Calcium binding site 1 out of 1 in the Engineered Cbm X-2 L110F in Complex with Branched Carbohydrate Xxxg.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Engineered Cbm X-2 L110F in Complex with Branched Carbohydrate Xxxg. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca201

b:14.7
occ:1.00
OE2 A:GLU52 2.3 18.2 1.0
O A:LYS55 2.4 14.9 1.0
OE2 A:GLU11 2.4 18.7 1.0
OD1 A:ASP160 2.4 13.5 1.0
O A:GLU52 2.4 18.3 1.0
O A:GLY9 2.5 13.9 1.0
OD2 A:ASP160 2.7 15.7 1.0
CG A:ASP160 2.9 13.1 1.0
HG3 A:GLU52 2.9 46.3 1.0
H A:LYS55 3.2 22.9 0.8
D A:LYS55 3.2 22.9 0.9
CD A:GLU52 3.2 27.6 1.0
HA3 A:GLY9 3.3 16.8 1.0
C A:GLU52 3.4 25.3 1.0
C A:GLY9 3.4 13.5 1.0
HG2 A:GLU11 3.5 18.2 1.0
CD A:GLU11 3.5 21.7 1.0
C A:LYS55 3.5 14.6 1.0
CG A:GLU52 3.6 38.6 1.0
HA2 A:GLY9 3.7 16.8 1.0
CA A:GLY9 3.7 14.0 1.0
HB1 A:ALA50 3.9 25.7 1.0
H A:GLU52 3.9 23.7 0.3
D A:GLU52 3.9 23.7 1.0
HA3 A:GLY53 3.9 22.4 1.0
N A:LYS55 3.9 19.1 1.0
CG A:GLU11 4.0 15.2 1.0
HB2 A:LYS55 4.1 21.7 1.0
HA A:VAL56 4.2 17.4 1.0
HG12 A:VAL56 4.2 18.1 1.0
CA A:LYS55 4.2 17.3 1.0
HG2 A:GLU52 4.2 46.3 1.0
CA A:GLU52 4.3 21.7 1.0
D A:GLY161 4.3 16.1 0.1
H A:GLY161 4.3 16.1 1.0
N A:GLY53 4.3 23.5 1.0
OE1 A:GLU52 4.3 33.8 1.0
HD2 A:PHE10 4.3 16.4 1.0
HB2 A:PHE10 4.4 15.6 1.0
HG3 A:GLU11 4.4 18.2 1.0
CB A:ASP160 4.4 12.5 1.0
CA A:GLY53 4.4 18.7 1.0
H A:ASN54 4.4 22.8 0.2
D A:ASN54 4.4 22.8 1.0
N A:GLU52 4.5 19.8 1.0
CB A:GLU52 4.5 37.2 1.0
OE1 A:GLU11 4.5 22.6 1.0
N A:VAL56 4.6 13.7 1.0
N A:ASN54 4.6 19.0 1.0
C A:GLY53 4.7 18.9 1.0
CB A:LYS55 4.7 18.1 1.0
N A:PHE10 4.7 12.1 1.0
HB2 A:ASP160 4.7 15.0 1.0
H A:GLU11 4.8 18.4 0.5
D A:GLU11 4.8 18.4 1.0
CB A:ALA50 4.8 21.4 1.0
HA A:ASP160 4.8 14.8 1.0
CA A:VAL56 4.9 14.5 1.0
HB3 A:ASP160 4.9 15.0 1.0
N A:GLY161 4.9 13.5 1.0
N A:GLU11 5.0 15.3 1.0
HB2 A:GLU52 5.0 44.6 1.0

Reference:

S.Z.Fisher, L.Von Schantz, M.Hakansson, D.T.Logan, M.Ohlin. Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions Between A Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand. Biochemistry V. 54 6435 2015.
ISSN: ISSN 0006-2960
PubMed: 26451738
DOI: 10.1021/ACS.BIOCHEM.5B01058
Page generated: Sat Dec 12 05:22:14 2020

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