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Calcium in PDB 3djl: Crystal Structure of Alkylation Response Protein E. Coli Aidb

Protein crystallography data

The structure of Crystal Structure of Alkylation Response Protein E. Coli Aidb, PDB code: 3djl was solved by B.F.Eichman, A.H.Metz, T.Bowles, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.63 / 1.70
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 84.989, 101.875, 137.566, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 17.9

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Alkylation Response Protein E. Coli Aidb (pdb code 3djl). 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 Alkylation Response Protein E. Coli Aidb, PDB code: 3djl:

Calcium binding site 1 out of 1 in 3djl

Go back to Calcium Binding Sites List in 3djl
Calcium binding site 1 out of 1 in the Crystal Structure of Alkylation Response Protein E. Coli Aidb


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 Alkylation Response Protein E. Coli Aidb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca601

b:35.6
occ:1.00
O A:HOH716 2.0 31.5 1.0
O A:HOH711 2.1 30.1 1.0
OE1 A:GLN333 2.4 29.7 1.0
O A:HOH701 2.4 43.1 1.0
O A:HOH1062 2.4 29.9 1.0
O A:HOH1061 2.7 37.0 1.0
CD A:GLN333 3.6 25.4 1.0
OE2 A:GLU525 3.8 37.2 1.0
O A:HOH1092 4.1 46.0 1.0
NE2 A:GLN333 4.3 27.7 1.0
OE1 A:GLU525 4.4 38.5 1.0
O A:GLN333 4.5 15.6 1.0
O A:HOH1091 4.5 47.2 1.0
CD A:ARG338 4.5 15.2 1.0
CD A:GLU525 4.6 34.1 1.0
O A:HOH1125 4.6 44.7 1.0
NE A:ARG338 4.6 17.9 1.0
O A:HOH871 4.6 29.0 1.0
CB A:GLN333 4.7 14.9 1.0
O A:HOH998 4.7 38.9 1.0
CG A:GLN333 4.7 17.9 1.0
O A:HOH847 4.8 26.6 1.0
CA A:GLN333 4.9 15.7 1.0

Reference:

T.Bowles, A.H.Metz, J.O'quin, Z.Wawrzak, B.F.Eichman. Structure and Dna Binding of Alkylation Response Protein Aidb. Proc.Natl.Acad.Sci.Usa V. 105 15299 2008.
ISSN: ISSN 0027-8424
PubMed: 18829440
DOI: 10.1073/PNAS.0806521105
Page generated: Sat Dec 12 04:08:58 2020

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