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Calcium in PDB 6z0e: HTRA1 Inactive Protease Domain S328A with Carasil Mutation R274Q

Protein crystallography data

The structure of HTRA1 Inactive Protease Domain S328A with Carasil Mutation R274Q, PDB code: 6z0e was solved by I.R.Vetter, P.Stege, L.Ingendahl, M.Ehrmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.02 / 2.60
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 109.86, 109.86, 114.4, 90, 90, 120
R / Rfree (%) 23.8 / 26.5

Calcium Binding Sites:

The binding sites of Calcium atom in the HTRA1 Inactive Protease Domain S328A with Carasil Mutation R274Q (pdb code 6z0e). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the HTRA1 Inactive Protease Domain S328A with Carasil Mutation R274Q, PDB code: 6z0e:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 6z0e

Go back to Calcium Binding Sites List in 6z0e
Calcium binding site 1 out of 2 in the HTRA1 Inactive Protease Domain S328A with Carasil Mutation R274Q


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of HTRA1 Inactive Protease Domain S328A with Carasil Mutation R274Q within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca401

b:42.1
occ:0.21
O A:HOH519 2.6 40.3 1.0
O A:HOH510 2.6 34.7 1.0
O A:HOH514 3.4 38.3 1.0
O A:HOH517 4.4 25.8 1.0
O A:ASP320 4.6 38.2 1.0
OD1 A:ASP320 4.8 43.0 1.0
O A:HOH520 4.9 49.9 0.3

Calcium binding site 2 out of 2 in 6z0e

Go back to Calcium Binding Sites List in 6z0e
Calcium binding site 2 out of 2 in the HTRA1 Inactive Protease Domain S328A with Carasil Mutation R274Q


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of HTRA1 Inactive Protease Domain S328A with Carasil Mutation R274Q within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca401

b:48.7
occ:0.25
O B:HOH513 2.6 38.5 1.0
O B:HOH509 2.6 50.1 1.0
O B:HOH503 4.2 46.9 1.0
O B:HOH508 4.5 37.1 1.0
O B:ASP320 4.6 47.6 1.0
OD1 B:ASP320 4.6 51.1 1.0

Reference:

L.Ingendahl, N.Beaufort, M.Kuszner, I.R.Vetter, P.Stege, Y.B.Ruiz-Blanco, K.Bravo-Rodriguez, C.Beuck, J.Schillinger, J.Rey, A.Roberti, B.Hagemeier, X.-Y.Hu, T.Clausen, E.Sanchez-Garcia, C.Schmuck, M.Dichgans, M.Ehrmann. Repair Strategies Addressing Pathogenic Protein Conformations To Be Published.
Page generated: Wed Jul 9 20:29:18 2025

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