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Calcium in PDB 4n9p: Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs V23T/L25A/V99T at Cryogenic Temperature

Enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs V23T/L25A/V99T at Cryogenic Temperature

All present enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs V23T/L25A/V99T at Cryogenic Temperature:
3.1.31.1;

Protein crystallography data

The structure of Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs V23T/L25A/V99T at Cryogenic Temperature, PDB code: 4n9p was solved by J.A.Caro, J.L.Schlessman, A.Heroux, B.Garcia-Moreno E., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.21 / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 31.234, 60.133, 38.340, 90.00, 94.72, 90.00
R / Rfree (%) 17.6 / 19.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs V23T/L25A/V99T at Cryogenic Temperature (pdb code 4n9p). 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 V23T/L25A/V99T at Cryogenic Temperature, PDB code: 4n9p:

Calcium binding site 1 out of 1 in 4n9p

Go back to Calcium Binding Sites List in 4n9p
Calcium binding site 1 out of 1 in the Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs V23T/L25A/V99T 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 V23T/L25A/V99T at Cryogenic Temperature within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca201

b:17.1
occ:1.00
 OD1 A:ASP40 2.7 15.8 1.0
O A:HOH318 2.8 15.5 1.0
OD2 A:ASP21 2.8 12.4 1.0
O A:THR41 2.9 15.5 1.0
O A:HOH324 2.9 18.0 1.0
OE2 A:GLU43 3.0 31.9 1.0
O5P A:THP202 3.2 11.5 1.0
O A:HOH337 3.6 27.0 1.0
CG A:ASP21 3.7 11.2 1.0
OD1 A:ASP21 3.8 13.1 1.0
CG A:ASP40 3.8 14.6 1.0
CD A:GLU43 4.0 31.4 1.0
C A:THR41 4.0 13.7 1.0
N A:THR41 4.0 11.5 1.0
NH2 A:ARG35 4.1 9.9 1.0
P2 A:THP202 4.1 12.2 1.0
O A:HOH311 4.1 16.3 1.0
O A:HOH388 4.1 26.7 1.0
OG1 A:THR41 4.1 13.3 1.0
O4P A:THP202 4.2 13.1 1.0
CA A:THR41 4.5 13.5 1.0
OD2 A:ASP40 4.5 20.4 1.0
OE1 A:GLU43 4.6 28.6 1.0
O6P A:THP202 4.6 14.7 1.0
O A:HOH371 4.6 23.1 1.0
CZ A:ARG35 4.6 8.5 1.0
CA A:ASP40 4.7 11.2 1.0
C A:ASP40 4.7 11.3 1.0
O A:HOH408 4.7 28.2 1.0
C A:PRO42 4.8 17.6 1.0
NE A:ARG35 4.8 8.7 1.0
CB A:ASP40 4.9 12.1 1.0
CG A:GLU43 4.9 27.4 1.0
O A:PRO42 4.9 18.8 1.0
N A:GLU43 4.9 20.9 1.0
CB A:THR41 5.0 11.8 1.0

Reference:

J.A.Caro, J.L.Schlessman, B.Garcia-Moreno E.. Cavities in Proteins To Be Published.
Page generated: Wed Jul 9 00:47:16 2025

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