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Calcium in PDB 3kpt: Crystal Structure of Bcpa, the Major Pilin Subunit of Bacillus Cereus

Protein crystallography data

The structure of Crystal Structure of Bcpa, the Major Pilin Subunit of Bacillus Cereus, PDB code: 3kpt was solved by C.B.Poor, J.M.Budzik, O.Schneewind, C.He, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.61 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.552, 73.862, 201.366, 90.00, 90.00, 90.00
R / Rfree (%) 23.1 / 27.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Bcpa, the Major Pilin Subunit of Bacillus Cereus (pdb code 3kpt). 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 Bcpa, the Major Pilin Subunit of Bacillus Cereus, PDB code: 3kpt:

Calcium binding site 1 out of 1 in 3kpt

Go back to Calcium Binding Sites List in 3kpt
Calcium binding site 1 out of 1 in the Crystal Structure of Bcpa, the Major Pilin Subunit of Bacillus Cereus


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 Bcpa, the Major Pilin Subunit of Bacillus Cereus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca599

b:48.9
occ:1.00
O B:HOH600 2.3 47.1 1.0
O B:LYS236 2.5 52.0 1.0
OE1 B:GLU238 2.7 52.3 1.0
OE2 B:GLU238 2.7 48.1 1.0
CD B:GLU238 3.1 50.0 1.0
C B:LYS236 3.7 46.6 1.0
O B:HOH816 4.0 53.7 1.0
O B:HOH619 4.1 48.1 1.0
CB B:LYS236 4.4 44.6 1.0
CA B:LYS236 4.5 41.9 1.0
CG B:GLU238 4.6 42.6 1.0
N B:ARG237 4.7 51.7 1.0
N B:LYS236 4.7 45.5 1.0
CA B:ARG237 4.8 50.3 1.0
N B:GLU238 4.8 47.6 1.0
O B:HOH633 4.9 56.9 1.0
CG2 B:THR235 4.9 39.7 1.0

Reference:

J.M.Budzik, C.B.Poor, K.F.Faull, J.P.Whitelegge, C.He, O.Schneewind. Intramolecular Amide Bonds Stabilize Pili on the Surface of Bacilli. Proc.Natl.Acad.Sci.Usa V. 106 19992 2009.
ISSN: ISSN 0027-8424
PubMed: 19903875
DOI: 10.1073/PNAS.0910887106
Page generated: Sat Dec 12 04:17:51 2020

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