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Calcium in PDB 3mz5: Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs L103A at Cryogenic Temperature

Enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs L103A at Cryogenic Temperature

All present enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs L103A at Cryogenic Temperature:
3.1.31.1;

Protein crystallography data

The structure of Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs L103A at Cryogenic Temperature, PDB code: 3mz5 was solved by J.A.Caro, J.L.Schlessman, E.B.Garcia-Moreno, A.Heroux, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.25 / 1.58
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 31.068, 60.504, 38.032, 90.00, 93.65, 90.00
R / Rfree (%) 19 / 23.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs L103A at Cryogenic Temperature (pdb code 3mz5). 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 Staphylococcal Nuclease Variant Delta+Phs L103A at Cryogenic Temperature, PDB code: 3mz5:

Calcium binding site 1 out of 1 in 3mz5

Go back to Calcium Binding Sites List in 3mz5
Calcium binding site 1 out of 1 in the Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs L103A at Cryogenic Temperature


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 Staphylococcal Nuclease Variant Delta+Phs L103A at Cryogenic Temperature within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca151

b:21.8
occ:1.00
 OD1 A:ASP40 2.7 19.6 1.0
O A:HOH154 2.8 18.9 1.0
O A:THR41 2.8 18.8 1.0
OD2 A:ASP21 2.8 17.2 1.0
O A:HOH155 2.9 21.0 1.0
O6P A:THP150 3.1 20.6 1.0
OE2 A:GLU43 3.1 37.8 1.0
O A:HOH198 3.6 29.7 1.0
CG A:ASP21 3.7 13.7 1.0
OD1 A:ASP21 3.8 17.0 1.0
CG A:ASP40 3.9 21.8 1.0
C A:THR41 3.9 18.6 1.0
N A:THR41 4.0 16.0 1.0
CD A:GLU43 4.0 36.4 1.0
O A:HOH196 4.0 24.2 1.0
O A:HOH217 4.1 32.8 1.0
P2 A:THP150 4.1 18.1 1.0
NH2 A:ARG35 4.1 13.3 1.0
O4P A:THP150 4.2 17.4 1.0
OG1 A:THR41 4.2 18.0 1.0
CA A:THR41 4.5 17.4 1.0
O5P A:THP150 4.6 21.0 1.0
OE1 A:GLU43 4.6 35.5 1.0
OD2 A:ASP40 4.6 26.9 1.0
O A:HOH165 4.6 25.2 1.0
CA A:ASP40 4.7 15.8 1.0
C A:ASP40 4.7 17.9 1.0
CZ A:ARG35 4.7 12.5 1.0
C A:PRO42 4.8 21.5 1.0
CG A:GLU43 4.9 30.8 1.0
NE A:ARG35 4.9 12.5 1.0
N A:GLU43 4.9 24.9 1.0
CB A:ASP40 4.9 16.8 1.0
O A:PRO42 4.9 23.0 1.0
CB A:THR41 5.0 16.9 1.0

Reference:

J.Roche, J.A.Caro, D.R.Norberto, P.Barthe, C.Roumestand, J.L.Schlessman, A.E.Garcia, B.Garcia-Moreno E, C.A.Royer. Cavities Determine the Pressure Unfolding of Proteins. Proc.Natl.Acad.Sci.Usa V. 109 6945 2012.
ISSN: ISSN 0027-8424
PubMed: 22496593
DOI: 10.1073/PNAS.1200915109
Page generated: Sat Jul 13 13:48:35 2024

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