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Calcium in PDB 8uf4: Crystal Structure of Wildtype Dystroglycan Proteolytic Domain (Juxtamembrane Domain)

Protein crystallography data

The structure of Crystal Structure of Wildtype Dystroglycan Proteolytic Domain (Juxtamembrane Domain), PDB code: 8uf4 was solved by M.J.M.Anderson, K.Shi, A.N.Hayward, C.Uhlens, R.L.Evans Iii, E.Grant, L.Greenberg, H.Aihara, W.R.Gordon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.43 / 2.43
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.945, 86.577, 128, 90, 90, 90
R / Rfree (%) 22.5 / 27.5

Other elements in 8uf4:

The structure of Crystal Structure of Wildtype Dystroglycan Proteolytic Domain (Juxtamembrane Domain) also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Wildtype Dystroglycan Proteolytic Domain (Juxtamembrane Domain) (pdb code 8uf4). 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 Crystal Structure of Wildtype Dystroglycan Proteolytic Domain (Juxtamembrane Domain), PDB code: 8uf4:

Calcium binding site 1 out of 1 in 8uf4

Go back to Calcium Binding Sites List in 8uf4
Calcium binding site 1 out of 1 in the Crystal Structure of Wildtype Dystroglycan Proteolytic Domain (Juxtamembrane Domain)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Wildtype Dystroglycan Proteolytic Domain (Juxtamembrane Domain) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca701

b:40.6
occ:1.00
OE1 A:GLU527 2.0 48.5 1.0
O A:HOH805 2.2 29.3 1.0
OD2 A:ASP581 2.2 38.7 1.0
OD1 A:ASN494 2.2 46.9 1.0
O A:GLN495 2.3 40.2 1.0
OD1 A:ASP525 2.4 42.7 1.0
OD2 A:ASP525 2.5 47.0 1.0
CG A:ASP525 2.7 43.3 1.0
CD A:GLU527 3.2 60.5 1.0
CG A:ASN494 3.3 43.5 1.0
CG A:ASP581 3.4 41.2 1.0
C A:GLN495 3.5 37.0 1.0
ND2 A:ASN494 3.7 44.4 1.0
N A:GLN495 3.9 57.5 1.0
CB A:ASP581 3.9 32.8 1.0
OE2 A:GLU527 3.9 63.0 1.0
CB A:ASP525 4.2 41.9 1.0
CA A:GLN495 4.3 42.4 1.0
CG A:GLU527 4.3 53.6 1.0
CD A:PRO497 4.3 42.4 1.0
CB A:GLU527 4.3 51.5 1.0
OD1 A:ASP581 4.4 41.6 1.0
N A:GLU527 4.5 49.1 1.0
N A:ARG496 4.6 44.6 1.0
N A:PRO497 4.6 34.1 1.0
CB A:ASN494 4.6 36.7 1.0
C A:ASN494 4.6 48.3 1.0
CG A:PRO497 4.6 31.7 1.0
C A:ARG496 4.7 40.5 1.0
CA A:ARG496 4.7 34.9 1.0
OD2 A:ASP528 4.7 51.3 1.0
CA A:ASN494 4.8 43.5 1.0
CB A:GLN495 4.8 43.8 1.0
N A:HIS526 4.9 45.1 1.0
CG A:ASP528 4.9 54.7 1.0

Reference:

M.J.M.Anderson, A.N.Hayward, C.Uhlens, K.Shi, M.R.Pawlak, E.Grant, L.Greenburg, H.Aihara, R.L.Evans Iii, W.R.Gordon. Structural and Functional Analysis of Dystroglycan Cell Surface Cleavage Reveals A Novel Regulation Mechanism To Be Published.
Page generated: Thu Jul 10 07:38:26 2025

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