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Calcium in PDB 1rio: Structure of Bacteriophage Lambda Ci-Ntd in Complex with Sigma-REGION4 of Thermus Aquaticus Bound to Dna

Protein crystallography data

The structure of Structure of Bacteriophage Lambda Ci-Ntd in Complex with Sigma-REGION4 of Thermus Aquaticus Bound to Dna, PDB code: 1rio was solved by D.Jain, B.E.Nickels, L.Sun, A.Hochschild, S.A.Darst, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.256, 71.269, 77.199, 90.00, 91.34, 90.00
R / Rfree (%) 21.6 / 25.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Bacteriophage Lambda Ci-Ntd in Complex with Sigma-REGION4 of Thermus Aquaticus Bound to Dna (pdb code 1rio). 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 Structure of Bacteriophage Lambda Ci-Ntd in Complex with Sigma-REGION4 of Thermus Aquaticus Bound to Dna, PDB code: 1rio:

Calcium binding site 1 out of 1 in 1rio

Go back to Calcium Binding Sites List in 1rio
Calcium binding site 1 out of 1 in the Structure of Bacteriophage Lambda Ci-Ntd in Complex with Sigma-REGION4 of Thermus Aquaticus Bound to Dna


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Bacteriophage Lambda Ci-Ntd in Complex with Sigma-REGION4 of Thermus Aquaticus Bound to Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:71.7
occ:1.00
O A:GLY42 2.2 38.7 1.0
O T:HOH44 2.6 37.6 1.0
O T:HOH45 2.8 50.6 1.0
O A:HOH306 2.9 45.7 1.0
O A:HOH311 3.4 0.1 1.0
C A:GLY42 3.4 39.6 1.0
CA A:GLY42 4.3 39.7 1.0
OP1 T:DT20 4.3 22.7 1.0
N A:MSE43 4.4 38.9 1.0
CA A:MSE43 4.5 38.9 1.0
OP1 T:DG19 4.8 21.6 1.0
CB A:MSE43 4.9 37.9 1.0

Reference:

D.Jain, B.E.Nickels, L.Sun, A.Hochschild, S.A.Darst. Structure of A Ternary Transcription Activation Complex. Mol.Cell V. 13 45 2004.
ISSN: ISSN 1097-2765
PubMed: 14731393
DOI: 10.1016/S1097-2765(03)00483-0
Page generated: Thu Jul 11 22:12:21 2024

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