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Calcium in PDB 7cof: Cholesterol Esterase From Burkholderia Stabilis (Orthorhombic Crystal Form)

Protein crystallography data

The structure of Cholesterol Esterase From Burkholderia Stabilis (Orthorhombic Crystal Form), PDB code: 7cof was solved by Y.Yasutake, T.Tamura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.01 / 1.08
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 58.241, 61.365, 147.177, 90.00, 90.00, 90.00
R / Rfree (%) 9.8 / 11.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Cholesterol Esterase From Burkholderia Stabilis (Orthorhombic Crystal Form) (pdb code 7cof). 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 Cholesterol Esterase From Burkholderia Stabilis (Orthorhombic Crystal Form), PDB code: 7cof:

Calcium binding site 1 out of 1 in 7cof

Go back to Calcium Binding Sites List in 7cof
Calcium binding site 1 out of 1 in the Cholesterol Esterase From Burkholderia Stabilis (Orthorhombic Crystal Form)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cholesterol Esterase From Burkholderia Stabilis (Orthorhombic Crystal Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca401

b:4.2
occ:1.00
OD1 A:ASP288 2.3 4.4 1.0
OD2 A:ASP242 2.3 5.1 1.0
O A:VAL296 2.3 4.8 1.0
O A:HOH536 2.3 4.8 1.0
O A:GLN292 2.4 4.5 1.0
O A:HOH566 2.4 5.5 1.0
HA A:ARG297 3.2 5.7 1.0
H A:LEU293 3.2 5.8 1.0
C A:GLN292 3.3 4.4 1.0
C A:VAL296 3.5 4.7 1.0
CG A:ASP288 3.5 4.0 1.0
CG A:ASP242 3.5 5.0 1.0
N A:LEU293 3.6 4.9 1.0
HA A:ASP288 3.7 4.9 1.0
CA A:ARG297 4.0 4.8 1.0
HG13 A:ILE287 4.0 10.4 1.0
HG11 A:VAL296 4.1 7.0 1.0
HB3 A:ARG297 4.2 6.9 1.0
N A:ARG297 4.2 4.8 1.0
HB A:VAL296 4.2 6.6 1.0
HB3 A:ASP242 4.3 6.2 1.0
CA A:ASP288 4.3 4.1 1.0
OD2 A:ASP288 4.3 4.3 1.0
N A:ASP288 4.3 4.1 1.0
OG A:SER244 4.3 5.4 1.0
H A:ASP288 4.3 4.9 1.0
HB2 A:ASP242 4.3 6.2 1.0
CB A:ASP242 4.4 5.2 1.0
OD1 A:ASN285 4.4 4.2 1.0
OD1 A:ASP242 4.4 5.0 1.0
O A:HOH544 4.4 4.7 1.0
ND2 A:ASN285 4.4 5.1 1.0
CB A:ASP288 4.4 4.0 1.0
OG1 A:THR245 4.5 4.8 1.0
CB A:ARG297 4.6 5.8 1.0
CA A:VAL296 4.6 5.1 1.0
HB1 A:ALA238 4.7 6.6 1.0
CA A:GLN292 4.7 4.4 1.0
HB2 A:ARG297 4.8 6.9 1.0
H A:GLN292 4.8 5.1 1.0
C A:ILE287 4.8 4.5 1.0
CB A:VAL296 4.8 5.5 1.0
HG12 A:ILE287 4.8 10.4 1.0
CG1 A:ILE287 4.8 8.7 1.0
CG A:ASN285 4.8 4.0 1.0
H A:VAL296 4.9 5.9 1.0
CG1 A:VAL296 4.9 5.8 1.0
HB3 A:ASP288 4.9 4.8 1.0
HD12 A:ILE287 5.0 10.2 1.0
N A:VAL296 5.0 5.0 1.0
N A:GLN292 5.0 4.2 1.0

Reference:

Y.Yasutake, K.Konishi, S.Muramatsu, K.Yoshida, S.Aburatani, S.I.Sakasegawa, T.Tamura. Bacterial Triacylglycerol Lipase Is A Potential Cholesterol Esterase: Identification of A Key Determinant For Sterol-Binding Specificity. Int.J.Biol.Macromol. V. 167 578 2021.
ISSN: ISSN 0141-8130
DOI: 10.1016/J.IJBIOMAC.2020.11.184
Page generated: Thu Jul 18 23:47:45 2024

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