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Zinc in PDB 4nqy: The Reduced Form of MJ0499

Enzymatic activity of The Reduced Form of MJ0499

All present enzymatic activity of The Reduced Form of MJ0499:
4.2.1.31; 4.2.1.33; 4.2.1.35;

Protein crystallography data

The structure of The Reduced Form of MJ0499, PDB code: 4nqy was solved by K.Y.Hwang, E.H.Lee, K.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.36 / 2.60
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 117.010, 117.010, 84.900, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 24.5

Zinc Binding Sites:

The binding sites of Zinc atom in the The Reduced Form of MJ0499 (pdb code 4nqy). 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 The Reduced Form of MJ0499, PDB code: 4nqy:

Zinc binding site 1 out of 1 in 4nqy

Go back to Zinc Binding Sites List in 4nqy
Zinc binding site 1 out of 1 in the The Reduced Form of MJ0499


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Reduced Form of MJ0499 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:82.1
occ:1.00
SG B:CYS365 2.4 69.4 1.0
SG A:CYS368 2.4 68.0 1.0
SG A:CYS365 2.4 69.2 1.0
SG B:CYS368 2.4 66.1 1.0
CB A:CYS365 3.1 43.6 1.0
CB B:CYS365 3.1 52.8 1.0
CB A:CYS368 3.4 57.6 1.0
CB B:CYS368 3.4 58.9 1.0
N A:CYS368 3.8 66.2 1.0
N B:CYS368 3.8 67.8 1.0
CA A:CYS368 4.0 62.7 1.0
CA B:CYS368 4.0 65.7 1.0
CB A:ASN362 4.3 67.7 1.0
CB B:ASN362 4.4 60.9 1.0
CA B:CYS365 4.5 61.8 1.0
CA A:CYS365 4.6 51.5 1.0
CB B:ALA367 4.6 65.4 1.0
CB A:ALA367 4.7 65.6 1.0
C B:ALA367 4.8 72.1 1.0
C A:ALA367 4.8 70.8 1.0
N A:ASN362 4.9 77.3 1.0
C B:CYS365 5.0 63.3 1.0
C A:CYS365 5.0 56.5 1.0
O B:CYS365 5.0 64.6 1.0
O A:CYS365 5.0 58.6 1.0

Reference:

E.H.Lee, K.Lee, K.Y.Hwang. Structural Characterization and Comparison of the Large Subunits of Ipm Isomerase and Homoaconitase From Methanococcus Jannaschii Acta Crystallogr.,Sect.D V. 70 922 2014.
ISSN: ISSN 0907-4449
PubMed: 24699638
DOI: 10.1107/S1399004713033762
Page generated: Sun Oct 27 03:19:20 2024

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