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Zinc in PDB 1gr0: Myo-Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis in Complex with Nad and Zinc.

Enzymatic activity of Myo-Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis in Complex with Nad and Zinc.

All present enzymatic activity of Myo-Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis in Complex with Nad and Zinc.:
5.5.1.4;

Protein crystallography data

The structure of Myo-Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis in Complex with Nad and Zinc., PDB code: 1gr0 was solved by R.A.Norman, J.Murray-Rust, N.Q.Mcdonald, Tb Structural Genomicsconsortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.79 / 1.95
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 116.195, 116.195, 64.544, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 23.9

Other elements in 1gr0:

The structure of Myo-Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis in Complex with Nad and Zinc. also contains other interesting chemical elements:

Arsenic (As) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Myo-Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis in Complex with Nad and Zinc. (pdb code 1gr0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Myo-Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis in Complex with Nad and Zinc., PDB code: 1gr0:

Zinc binding site 1 out of 1 in 1gr0

Go back to Zinc Binding Sites List in 1gr0
Zinc binding site 1 out of 1 in the Myo-Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis in Complex with Nad and Zinc.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Myo-Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis in Complex with Nad and Zinc. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1200

b:31.6
occ:0.50
 N7N A:NAD1000 2.1 24.0 1.0
O2N A:NAD1000 2.2 27.0 1.0
O A:HOH2170 2.2 24.3 1.0
OG A:SER311 2.4 27.7 1.0
SG A:CYS26 3.2 24.4 1.0
C7N A:NAD1000 3.4 26.7 1.0
PN A:NAD1000 3.5 24.5 1.0
CB A:SER311 3.6 25.3 1.0
CA A:SER311 3.7 25.4 1.0
O5D A:NAD1000 3.9 23.4 1.0
N A:SER311 3.9 23.6 1.0
O1N A:NAD1000 3.9 26.4 1.0
C2N A:NAD1000 4.1 28.5 1.0
OD1 A:ASP282 4.1 24.7 1.0
ND2 A:ASN233 4.2 25.0 1.0
OD2 A:ASP235 4.2 29.0 1.0
O A:HOH2002 4.2 23.3 1.0
C3N A:NAD1000 4.3 27.9 1.0
CB A:ASN25 4.3 22.5 1.0
O7N A:NAD1000 4.3 31.4 1.0
OD2 A:ASP310 4.3 32.6 1.0
N A:CYS26 4.4 20.6 1.0
CB A:ASP235 4.5 26.6 1.0
C A:ASP310 4.5 23.9 1.0
CB A:CYS26 4.6 20.4 1.0
CG A:ASP310 4.6 31.2 1.0
CG A:ASP235 4.7 28.6 1.0
CB A:ASP310 4.7 26.9 1.0
O3 A:NAD1000 4.8 23.9 1.0
CA A:CYS26 4.8 19.9 1.0
O A:ASP310 4.9 21.3 1.0
C5D A:NAD1000 4.9 23.2 1.0
C A:ASN25 5.0 20.6 1.0

Reference:

R.A.Norman, M.S.B.Mcalister, J.Murray-Rust, F.Movahedzadeh, N.G.Stoker, N.Q.Mcdonald. Crystal Structure of Inositol 1-Phosphate Synthase From Mycobacterium Tuberculosis, A Key Enzyme in Phosphatidylinositol Synthesis Structure V. 10 393 2002.
ISSN: ISSN 0969-2126
PubMed: 12005437
DOI: 10.1016/S0969-2126(02)00718-9
Page generated: Sun Oct 13 01:40:40 2024

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