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Calcium in PDB 2x0h: BTGH84 Michaelis Complex

Enzymatic activity of BTGH84 Michaelis Complex

All present enzymatic activity of BTGH84 Michaelis Complex:
3.2.1.52;

Protein crystallography data

The structure of BTGH84 Michaelis Complex, PDB code: 2x0h was solved by Y.He, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.08 / 2.21
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.630, 163.147, 224.549, 90.00, 90.00, 90.00
R / Rfree (%) 19.42 / 22.589

Other elements in 2x0h:

The structure of BTGH84 Michaelis Complex also contains other interesting chemical elements:

Fluorine (F) 8 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the BTGH84 Michaelis Complex (pdb code 2x0h). 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 BTGH84 Michaelis Complex, PDB code: 2x0h:

Calcium binding site 1 out of 1 in 2x0h

Go back to Calcium Binding Sites List in 2x0h
Calcium binding site 1 out of 1 in the BTGH84 Michaelis Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of BTGH84 Michaelis Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1716

b:30.6
occ:0.75
OE1 B:GLU61 2.2 32.5 1.0
OD2 B:ASP64 2.4 32.0 1.0
O B:HOH2045 2.4 36.9 1.0
O B:HOH2032 2.4 40.9 1.0
O B:GLU32 2.5 37.9 1.0
OD1 B:ASP64 2.6 34.7 1.0
O B:HOH2086 2.6 51.2 1.0
CG B:ASP64 2.9 33.7 1.0
CD B:GLU61 3.4 27.0 1.0
C B:GLU32 3.5 38.9 1.0
CB B:GLU61 4.0 29.1 1.0
O B:HOH2048 4.0 49.9 1.0
CG B:GLU61 4.1 28.5 1.0
CA B:ALA33 4.3 32.7 1.0
N B:ALA33 4.3 35.6 1.0
OE2 B:GLU61 4.4 30.0 1.0
CB B:ASP64 4.4 32.6 1.0
N B:GLU61 4.4 28.1 1.0
CA B:GLU32 4.5 43.1 1.0
CB B:GLU32 4.5 45.1 1.0
OE2 B:GLU97 4.6 47.3 1.0
C B:ALA33 4.7 32.2 1.0
CA B:GLU61 4.8 27.9 1.0
N B:ASN34 4.9 29.5 1.0

Reference:

Y.He, M.S.Macauley, K.A.Stubbs, D.J.Vocadlo, G.J.Davies. Visualizing the Reaction Coordinate of An O-Glcnac Hydrolase J.Am.Chem.Soc. V. 132 1807 2010.
ISSN: ISSN 0002-7863
PubMed: 20067256
DOI: 10.1021/JA9086769
Page generated: Fri Jul 12 18:59:40 2024

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