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Calcium in PDB 1p3h: Crystal Structure of the Mycobacterium Tuberculosis Chaperonin 10 Tetradecamer

Protein crystallography data

The structure of Crystal Structure of the Mycobacterium Tuberculosis Chaperonin 10 Tetradecamer, PDB code: 1p3h was solved by M.M.Roberts, A.R.Coker, G.Fossati, P.Mascagni, A.R.M.Coates, S.P.Wood, Tbstructural Genomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 76.460, 87.930, 124.390, 90.00, 106.78, 90.00
R / Rfree (%) 25.9 / 28

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Mycobacterium Tuberculosis Chaperonin 10 Tetradecamer (pdb code 1p3h). 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 the Mycobacterium Tuberculosis Chaperonin 10 Tetradecamer, PDB code: 1p3h:

Calcium binding site 1 out of 1 in 1p3h

Go back to Calcium Binding Sites List in 1p3h
Calcium binding site 1 out of 1 in the Crystal Structure of the Mycobacterium Tuberculosis Chaperonin 10 Tetradecamer


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 the Mycobacterium Tuberculosis Chaperonin 10 Tetradecamer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca200

b:73.1
occ:1.00
O A:HOH203 2.4 40.0 1.0
OD1 B:ASP51 2.9 71.2 1.0
O A:ASP53 3.3 91.6 1.0
OE1 B:GLU55 3.6 77.8 1.0
C A:ASP53 3.8 91.2 1.0
CG B:ASP51 3.8 70.9 1.0
CB A:ASP53 4.1 89.2 1.0
CB B:LYS56 4.3 66.2 1.0
CA A:ASP53 4.3 90.9 1.0
CB B:ASP51 4.3 67.2 1.0
N A:GLY54 4.4 92.7 1.0
N B:LYS56 4.7 66.4 1.0
CB B:GLU55 4.7 70.8 1.0
OD2 B:ASP51 4.7 71.0 1.0
CA A:GLY54 4.7 89.8 1.0
C A:GLY54 4.7 89.0 1.0
CD B:GLU55 4.8 72.6 1.0
N A:GLU55 4.9 88.0 1.0

Reference:

M.M.Roberts, A.R.Coker, G.Fossati, P.Mascagni, A.R.M.Coates, S.P.Wood. Mycobacterium Tuberculosis Chaperonin 10 Heptamers Self-Associate Through Their Biologically Active Loops J.Bacteriol. V. 185 4172 2003.
ISSN: ISSN 0021-9193
PubMed: 12837792
DOI: 10.1128/JB.185.14.4172-4185.2003
Page generated: Thu Jul 11 13:39:04 2024

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