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Calcium in PDB 8frr: Wild-Type Myocilin Olfactomedin Domain

Protein crystallography data

The structure of Wild-Type Myocilin Olfactomedin Domain, PDB code: 8frr was solved by M.T.Ma, R.L.Lieberman, D.J.E.Huard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.91 / 1.27
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.468, 50.527, 50.873, 90, 96.25, 90
R / Rfree (%) 14 / 15.5

Other elements in 8frr:

The structure of Wild-Type Myocilin Olfactomedin Domain also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Wild-Type Myocilin Olfactomedin Domain (pdb code 8frr). 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 Wild-Type Myocilin Olfactomedin Domain, PDB code: 8frr:

Calcium binding site 1 out of 1 in 8frr

Go back to Calcium Binding Sites List in 8frr
Calcium binding site 1 out of 1 in the Wild-Type Myocilin Olfactomedin Domain


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Wild-Type Myocilin Olfactomedin Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca602

b:7.6
occ:1.00
OD1 A:ASP478 2.3 10.2 1.0
OD2 A:ASP380 2.4 9.4 1.0
O A:ALA429 2.4 8.3 1.0
O A:ILE477 2.4 8.4 1.0
O A:HOH802 2.5 8.6 1.0
OD1 A:ASN428 2.5 8.5 1.0
O A:HOH821 2.5 11.1 1.0
OD1 A:ASP380 3.0 9.8 1.0
CG A:ASP380 3.0 9.6 1.0
H A:ALA429 3.3 10.0 1.0
C A:ILE477 3.5 7.7 1.0
HA A:ASP478 3.5 9.5 1.0
CG A:ASP478 3.6 9.7 1.0
H A:ILE477 3.6 9.1 1.0
C A:ALA429 3.6 8.1 1.0
CG A:ASN428 3.6 8.2 1.0
HB3 A:PHE430 3.8 10.8 1.0
HH A:TYR371 3.9 11.5 1.0
NA A:NA603 4.0 9.7 1.0
HD21 A:ASN428 4.1 10.8 1.0
HA A:PHE430 4.1 10.6 1.0
N A:ALA429 4.1 8.3 1.0
CA A:ASP478 4.2 7.9 1.0
N A:ASP478 4.2 8.0 1.0
ND2 A:ASN428 4.3 9.0 1.0
N A:ILE477 4.3 7.6 1.0
HE2 A:TYR371 4.4 10.4 1.0
OD2 A:ASP478 4.4 12.0 1.0
O A:HOH744 4.4 10.1 1.0
HD12 A:ILE391 4.5 13.6 1.0
O A:HOH896 4.5 11.1 1.0
CA A:ILE477 4.5 7.9 1.0
CB A:ASP478 4.5 8.9 1.0
OH A:TYR371 4.5 9.6 1.0
HB A:ILE477 4.5 10.4 1.0
CA A:ALA429 4.5 9.2 1.0
CB A:ASP380 4.5 8.8 1.0
N A:PHE430 4.5 8.4 1.0
O A:HOH831 4.5 9.9 1.0
HB3 A:ASN428 4.6 10.1 1.0
CA A:PHE430 4.6 8.9 1.0
CB A:PHE430 4.6 9.0 1.0
CB A:ASN428 4.7 8.5 1.0
HB3 A:ASP380 4.8 10.5 1.0
O A:LEU381 4.8 9.0 1.0
HD2 A:PHE430 4.8 15.3 1.0
HB2 A:ASP380 4.8 10.5 1.0
HB3 A:ALA429 4.9 11.8 1.0
CE2 A:TYR371 4.9 8.7 1.0
H A:ASP478 5.0 9.6 1.0

Reference:

E.G.Saccuzzo, M.D.Mebrat, H.F.Scelsi, M.Kim, M.T.Ma, X.Su, S.E.Hill, E.Rheaume, R.Li, M.P.Torres, J.C.Gumbart, W.D.Van Horn, R.L.Lieberman. Competition Between Inside-Out Unfolding and Pathogenic Aggregation in An Amyloid-Forming Beta-Propeller. Nat Commun V. 15 155 2024.
ISSN: ESSN 2041-1723
PubMed: 38168102
DOI: 10.1038/S41467-023-44479-2
Page generated: Thu Jul 10 04:46:39 2025

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