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Zinc in PDB 1efz: Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity

Enzymatic activity of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity

All present enzymatic activity of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity:
2.4.2.29;

Protein crystallography data

The structure of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity, PDB code: 1efz was solved by U.Gradler, R.Ficner, G.A.Garcia, M.T.Stubbs, G.Klebe, K.Reuter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 71.00 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.600, 65.040, 70.740, 90.00, 96.25, 90.00
R / Rfree (%) 16.1 / 19.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity (pdb code 1efz). 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 Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity, PDB code: 1efz:

Zinc binding site 1 out of 1 in 1efz

Go back to Zinc Binding Sites List in 1efz
Zinc binding site 1 out of 1 in the Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:17.3
occ:1.00
 ND1 A:HIS349 2.2 9.9 1.0
SG A:CYS318 2.3 17.0 1.0
SG A:CYS323 2.3 14.6 1.0
SG A:CYS320 2.3 12.8 1.0
CE1 A:HIS349 3.0 12.6 1.0
CB A:CYS318 3.1 16.1 1.0
CG A:HIS349 3.3 8.3 1.0
CB A:CYS323 3.3 12.8 1.0
CB A:CYS320 3.3 11.0 1.0
CB A:HIS349 3.8 9.7 1.0
N A:CYS323 3.9 13.2 1.0
CA A:HIS349 4.1 10.3 1.0
N A:CYS320 4.1 16.1 1.0
NE2 A:HIS349 4.2 12.6 1.0
CA A:CYS320 4.2 13.1 1.0
CA A:CYS323 4.2 14.4 1.0
CD2 A:HIS349 4.3 10.4 1.0
CA A:CYS318 4.5 20.5 1.0
O A:HIS349 4.5 11.1 1.0
O A:CYS320 4.6 10.4 1.0
C A:CYS320 4.6 11.2 1.0
C A:CYS318 4.7 20.2 1.0
C A:HIS349 4.7 11.9 1.0
CB A:VAL322 4.8 13.7 1.0
O A:CYS318 4.9 20.2 1.0
C A:VAL322 5.0 14.2 1.0

Reference:

U.Gradler, R.Ficner, G.A.Garcia, M.T.Stubbs, G.Klebe, K.Reuter. Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna-Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity. Febs Lett. V. 454 142 1999.
ISSN: ISSN 0014-5793
PubMed: 10413112
DOI: 10.1016/S0014-5793(99)00793-0
Page generated: Sun Oct 13 00:13:21 2024

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