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Calcium in PDB 3gq8: Crystal Structure of the Bacteriophage PHI29 Gene Product 12 N- Terminal Fragment in Complex with 2-(N-Cyclohexylamino)Ethane Sulfonic Acid (Ches)

Protein crystallography data

The structure of Crystal Structure of the Bacteriophage PHI29 Gene Product 12 N- Terminal Fragment in Complex with 2-(N-Cyclohexylamino)Ethane Sulfonic Acid (Ches), PDB code: 3gq8 was solved by Y.Xiang, M.G.Rossmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.24 / 2.00
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 90.841, 90.841, 586.952, 90.00, 90.00, 120.00
R / Rfree (%) 16.9 / 19.6

Other elements in 3gq8:

The structure of Crystal Structure of the Bacteriophage PHI29 Gene Product 12 N- Terminal Fragment in Complex with 2-(N-Cyclohexylamino)Ethane Sulfonic Acid (Ches) also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Bacteriophage PHI29 Gene Product 12 N- Terminal Fragment in Complex with 2-(N-Cyclohexylamino)Ethane Sulfonic Acid (Ches) (pdb code 3gq8). 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 the Bacteriophage PHI29 Gene Product 12 N- Terminal Fragment in Complex with 2-(N-Cyclohexylamino)Ethane Sulfonic Acid (Ches), PDB code: 3gq8:

Calcium binding site 1 out of 1 in 3gq8

Go back to Calcium Binding Sites List in 3gq8
Calcium binding site 1 out of 1 in the Crystal Structure of the Bacteriophage PHI29 Gene Product 12 N- Terminal Fragment in Complex with 2-(N-Cyclohexylamino)Ethane Sulfonic Acid (Ches)


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 the Bacteriophage PHI29 Gene Product 12 N- Terminal Fragment in Complex with 2-(N-Cyclohexylamino)Ethane Sulfonic Acid (Ches) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1

b:21.8
occ:1.00
OD2 A:ASP279 2.3 23.1 1.0
O A:ASN305 2.3 21.2 1.0
OE2 A:GLU310 2.3 19.3 1.0
OD1 A:ASP280 2.4 20.4 1.0
OD2 A:ASP280 2.5 18.2 1.0
O1 A:CO3694 2.5 23.8 1.0
O2 A:CO3694 2.6 24.7 1.0
CG A:ASP280 2.8 20.2 1.0
C A:CO3694 2.8 24.8 1.0
CG A:ASP279 3.3 22.9 1.0
CD A:GLU310 3.3 22.0 1.0
C A:ASN305 3.5 20.8 1.0
ND2 A:ASN305 3.6 21.7 1.0
OE1 A:GLU310 3.7 22.9 1.0
OD1 A:ASP279 3.8 27.2 1.0
ND2 A:ASN307 3.9 16.7 1.0
O3 A:CO3694 4.0 25.2 1.0
CG A:ASN305 4.0 21.3 1.0
CB A:ASN305 4.1 21.2 1.0
MG A:MG692 4.2 23.7 1.0
O A:HOH776 4.2 39.5 1.0
CB A:ASP280 4.3 19.6 1.0
O A:HOH80 4.3 18.6 1.0
C A:ASP279 4.5 20.7 1.0
CA A:ASN305 4.5 21.2 1.0
N A:CYS306 4.5 20.1 1.0
CB A:ASP279 4.5 21.8 1.0
N A:ASN307 4.5 17.8 1.0
CA A:CYS306 4.5 19.9 1.0
N A:ASP280 4.6 19.8 1.0
CG A:GLU310 4.6 17.4 1.0
CG A:ASN307 4.7 18.8 1.0
O A:ASP279 4.7 19.8 1.0
CA A:ASP279 4.8 20.9 1.0
OD1 A:ASN305 4.9 20.4 1.0
CB A:GLU310 4.9 16.2 1.0
CA A:ASP280 4.9 19.8 1.0
CB A:ASN307 5.0 17.5 1.0

Reference:

Y.Xiang, P.G.Leiman, L.Li, S.Grimes, D.L.Anderson, M.G.Rossmann. Crystallographic Insights Into the Autocatalytic Assembly Mechanism of A Bacteriophage Tail Spike. Mol.Cell V. 34 375 2009.
ISSN: ISSN 1097-2765
PubMed: 19450535
DOI: 10.1016/J.MOLCEL.2009.04.009
Page generated: Sat Jul 13 10:45:54 2024

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