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Calcium in PDB 3dhq: Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs A90R at Cryogenic Temperature

Enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs A90R at Cryogenic Temperature

All present enzymatic activity of Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs A90R at Cryogenic Temperature:
3.1.31.1;

Protein crystallography data

The structure of Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs A90R at Cryogenic Temperature, PDB code: 3dhq was solved by M.J.Harms, J.L.Schlessman, E.B.Garcia-Moreno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.30 / 2.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 30.931, 60.603, 38.421, 90.00, 93.93, 90.00
R / Rfree (%) 20.8 / 27.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs A90R at Cryogenic Temperature (pdb code 3dhq). 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 A90R at Cryogenic Temperature, PDB code: 3dhq:

Calcium binding site 1 out of 1 in 3dhq

Go back to Calcium Binding Sites List in 3dhq
Calcium binding site 1 out of 1 in the Crystal Structure of Staphylococcal Nuclease Variant Delta+Phs A90R 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 A90R at Cryogenic Temperature within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca150

b:21.4
occ:1.00
 O A:HOH197 2.7 25.8 1.0
OD2 A:ASP21 2.7 20.4 1.0
OD1 A:ASP40 2.8 25.5 1.0
O A:THR41 2.9 25.3 1.0
O6P A:THP151 3.0 23.6 1.0
OE2 A:GLU43 3.0 38.4 1.0
O A:HOH199 3.1 22.6 1.0
CG A:ASP21 3.6 20.3 1.0
CG A:ASP40 3.7 23.6 1.0
O A:HOH154 3.7 23.1 1.0
O A:HOH206 3.8 41.5 1.0
OD1 A:ASP21 3.8 22.1 1.0
NH2 A:ARG35 3.9 16.5 1.0
C A:THR41 4.0 25.1 1.0
CD A:GLU43 4.0 38.4 1.0
P2 A:THP151 4.0 24.1 1.0
N A:THR41 4.1 23.6 1.0
OG1 A:THR41 4.1 21.6 1.0
OD2 A:ASP40 4.2 22.0 1.0
O5P A:THP151 4.2 23.0 1.0
O A:HOH173 4.4 23.6 1.0
CZ A:ARG35 4.5 18.0 1.0
CA A:THR41 4.6 23.5 1.0
O A:HOH178 4.6 25.9 1.0
OE1 A:GLU43 4.6 39.2 1.0
CA A:ASP40 4.7 21.8 1.0
C A:ASP40 4.7 22.3 1.0
O4P A:THP151 4.7 25.9 1.0
CB A:ASP40 4.8 22.0 1.0
NE A:ARG35 4.8 15.1 1.0
C A:PRO42 4.9 29.0 1.0
N A:GLU43 4.9 30.4 1.0
O A:PRO42 5.0 29.1 1.0
CG A:GLU43 5.0 36.0 1.0
CB A:THR41 5.0 23.2 1.0

Reference:

M.J.Harms, J.L.Schlessman, G.R.Sue, B.Garcia-Moreno E. Arginine Residues at Internal Positions in A Protein Are Always Charged. Proc.Natl.Acad.Sci.Usa V. 108 18954 2011.
ISSN: ISSN 0027-8424
PubMed: 22080604
DOI: 10.1073/PNAS.1104808108
Page generated: Sat Jul 13 09:03:06 2024

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