Zinc in PDB 8x4i: Crystal Structure of the D117A Mutant of DIMT1 in Complex with 5'- Methylthioadenosine From Pyrococcus Horikoshii

Enzymatic activity of Crystal Structure of the D117A Mutant of DIMT1 in Complex with 5'- Methylthioadenosine From Pyrococcus Horikoshii

All present enzymatic activity of Crystal Structure of the D117A Mutant of DIMT1 in Complex with 5'- Methylthioadenosine From Pyrococcus Horikoshii:
2.1.1.182;

Protein crystallography data

The structure of Crystal Structure of the D117A Mutant of DIMT1 in Complex with 5'- Methylthioadenosine From Pyrococcus Horikoshii, PDB code: 8x4i was solved by S.Saha, A.Dutta, S.P.Kanaujia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 62.54 / 3.30
Space group P 6
Cell size a, b, c (Å), α, β, γ (°) 124.92, 124.92, 36.81, 90, 90, 120
R / Rfree (%) 20.1 / 28.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the D117A Mutant of DIMT1 in Complex with 5'- Methylthioadenosine From Pyrococcus Horikoshii (pdb code 8x4i). 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 Crystal Structure of the D117A Mutant of DIMT1 in Complex with 5'- Methylthioadenosine From Pyrococcus Horikoshii, PDB code: 8x4i:

Zinc binding site 1 out of 1 in 8x4i

Go back to Zinc Binding Sites List in 8x4i
Zinc binding site 1 out of 1 in the Crystal Structure of the D117A Mutant of DIMT1 in Complex with 5'- Methylthioadenosine From Pyrococcus Horikoshii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the D117A Mutant of DIMT1 in Complex with 5'- Methylthioadenosine From Pyrococcus Horikoshii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:79.8
occ:1.00
 ND1 A:HIS231 2.3 95.5 1.0
O A:HOH402 2.5 58.2 1.0
O A:HOH403 2.6 67.3 1.0
CB A:HIS231 3.0 96.3 1.0
CG A:HIS231 3.0 97.6 1.0
CE1 A:HIS231 3.5 99.9 1.0
CA A:HIS231 3.9 91.2 1.0
CD2 A:HIS231 4.2 98.2 1.0
NE2 A:HIS231 4.4 103.0 1.0
C A:HIS231 4.6 84.5 1.0
O A:HIS231 5.0 75.5 1.0
CE A:LYS234 5.0 76.2 1.0

Reference:

S.Saha, S.P.Kanaujia. Structural and Functional Characterization of Archaeal DIMT1 Unveils Distinct Protein Dynamics Essential For Efficient Catalysis. Structure 2024.
ISSN: ISSN 0969-2126
PubMed: 39146930
DOI: 10.1016/J.STR.2024.07.013
Page generated: Thu Oct 31 13:49:09 2024

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