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Calcium in PDB 1oto: Calcium-Binding Mutant of the Internalin B Lrr Domain

Protein crystallography data

The structure of Calcium-Binding Mutant of the Internalin B Lrr Domain, PDB code: 1oto was solved by M.Marino, J.Copp, S.Dramsi, T.Chapman, P.Van Der Geer, P.Cossart, P.Ghosh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.96
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.988, 56.125, 83.414, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23

Calcium Binding Sites:

The binding sites of Calcium atom in the Calcium-Binding Mutant of the Internalin B Lrr Domain (pdb code 1oto). 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 Calcium-Binding Mutant of the Internalin B Lrr Domain, PDB code: 1oto:

Calcium binding site 1 out of 1 in 1oto

Go back to Calcium Binding Sites List in 1oto
Calcium binding site 1 out of 1 in the Calcium-Binding Mutant of the Internalin B Lrr Domain


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Calcium-Binding Mutant of the Internalin B Lrr Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca250

b:57.4
occ:1.00
O A:HOH371 1.7 42.5 1.0
O A:HOH262 2.2 46.6 1.0
O A:PRO49 2.2 32.6 1.0
O A:HOH265 2.4 65.2 1.0
OD1 A:ASP51 2.5 41.3 1.0
O A:HOH330 2.6 39.2 1.0
O A:HOH264 2.9 36.2 1.0
CG A:ASP51 3.3 29.4 1.0
C A:PRO49 3.4 29.2 1.0
O A:HOH263 3.4 71.4 1.0
OD2 A:ASP51 3.5 52.6 1.0
O A:HOH316 3.9 51.8 1.0
CA A:PRO49 4.0 29.7 1.0
N A:ASP51 4.1 29.5 1.0
N A:ASP50 4.4 24.4 1.0
CB A:ASP51 4.5 28.9 1.0
C A:ASP50 4.6 32.5 1.0
CA A:ASP51 4.6 30.2 1.0
O A:HOH287 4.7 56.5 1.0
CA A:ASP50 4.7 27.4 1.0
O A:PHE48 4.8 21.4 1.0
CB A:PRO49 4.9 28.2 1.0

Reference:

M.Marino, M.Banerjee, J.Copp, S.Dramsi, T.Chapman, P.Van Der Geer, P.Cossart, P.Ghosh. Characterization of the Calcium-Binding Sites of Listeria Monocytogenes Inlb Biochem.Biophys.Res.Commun. V. 316 379 2004.
ISSN: ISSN 0006-291X
PubMed: 15020228
DOI: 10.1016/J.BBRC.2004.02.064
Page generated: Thu Jul 11 13:30:56 2024

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