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Calcium in PDB 2jcg: Apo Form of the Catabolite Control Protein A (Ccpa) From Bacillus Megaterium, with the Dna Binding Domain

Protein crystallography data

The structure of Apo Form of the Catabolite Control Protein A (Ccpa) From Bacillus Megaterium, with the Dna Binding Domain, PDB code: 2jcg was solved by R.K.Singh, S.Panjikar, G.J.Palm, W.Hinrichs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.60 / 2.60
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.450, 74.450, 238.840, 90.00, 90.00, 120.00
R / Rfree (%) 22.9 / 29.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Apo Form of the Catabolite Control Protein A (Ccpa) From Bacillus Megaterium, with the Dna Binding Domain (pdb code 2jcg). 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 Apo Form of the Catabolite Control Protein A (Ccpa) From Bacillus Megaterium, with the Dna Binding Domain, PDB code: 2jcg:

Calcium binding site 1 out of 1 in 2jcg

Go back to Calcium Binding Sites List in 2jcg
Calcium binding site 1 out of 1 in the Apo Form of the Catabolite Control Protein A (Ccpa) From Bacillus Megaterium, with the Dna Binding Domain


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Apo Form of the Catabolite Control Protein A (Ccpa) From Bacillus Megaterium, with the Dna Binding Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1333

b:57.4
occ:1.00
OE1 A:GLU231 2.4 44.3 1.0
OE2 A:GLU235 2.8 56.1 1.0
CD A:GLU231 3.4 42.7 1.0
CD A:GLU235 3.8 58.0 1.0
OE2 A:GLU231 3.9 37.2 1.0
OE1 A:GLU235 4.1 59.7 1.0
CG A:GLU231 4.6 46.1 1.0

Reference:

R.K.Singh, G.J.Palm, S.Panjikar, W.Hinrichs. Structure of the Apo Form of the Catabolite Control Protein A (Ccpa) From Bacillus Megaterium with A Dna-Binding Domain. Acta Crystallogr.,Sect.F V. 63 253 2007.
ISSN: ESSN 1744-3091
PubMed: 17401189
DOI: 10.1107/S1744309107008949
Page generated: Tue Jul 8 06:34:21 2025

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