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Zinc in PDB 7eev: Utp Cyclohydrolase

Protein crystallography data

The structure of Utp Cyclohydrolase, PDB code: 7eev was solved by H.Zhang, Y.Zhang, Z.Yuchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.56 / 2.15
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 114.646, 114.646, 282.713, 90, 90, 120
R / Rfree (%) 13.4 / 16.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Utp Cyclohydrolase (pdb code 7eev). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Utp Cyclohydrolase, PDB code: 7eev:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7eev

Go back to Zinc Binding Sites List in 7eev
Zinc binding site 1 out of 2 in the Utp Cyclohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Utp Cyclohydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:20.2
occ:1.00
O A:HOH813 2.0 19.7 1.0
SG A:CYS265 2.3 19.3 1.0
SG A:CYS263 2.3 20.4 1.0
SG A:CYS252 2.3 18.7 1.0
CB A:CYS252 3.1 17.5 1.0
CB A:CYS263 3.2 17.4 1.0
CB A:CYS265 3.3 16.5 1.0
H2'1 A:DUT501 3.6 35.8 0.8
H5'2 A:DUT501 3.8 35.6 0.8
CB A:SER255 3.9 18.5 1.0
O A:HOH728 4.0 22.5 1.0
NZ A:LYS303 4.2 22.2 1.0
N A:CYS265 4.3 18.8 1.0
CA A:CYS265 4.4 20.9 1.0
C2' A:DUT501 4.5 29.8 0.8
CA A:CYS252 4.6 16.0 1.0
CA A:CYS263 4.6 19.2 1.0
OG A:SER255 4.6 18.2 1.0
N1 A:DUT501 4.7 34.1 0.8
H2'2 A:DUT501 4.7 35.8 0.8
CE A:LYS303 4.8 24.0 1.0
C6 A:DUT501 4.8 33.9 0.8
OH A:TYR307 4.9 18.1 1.0
C A:CYS263 4.9 20.9 1.0
C5' A:DUT501 4.9 29.6 0.8
C1' A:DUT501 5.0 23.8 0.8
N A:SER255 5.0 18.2 1.0

Zinc binding site 2 out of 2 in 7eev

Go back to Zinc Binding Sites List in 7eev
Zinc binding site 2 out of 2 in the Utp Cyclohydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Utp Cyclohydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn502

b:20.6
occ:1.00
O B:HOH902 1.9 19.4 1.0
SG B:CYS265 2.3 15.7 1.0
SG B:CYS263 2.3 17.9 1.0
SG B:CYS252 2.3 16.1 1.0
CB B:CYS252 3.1 18.5 1.0
CB B:CYS263 3.2 14.6 1.0
CB B:CYS265 3.3 15.2 1.0
H2'1 B:DUT501 3.6 32.0 0.8
CB B:SER255 3.8 15.3 1.0
O B:HOH739 4.0 19.6 1.0
H5'2 B:DUT501 4.2 30.5 0.8
N B:CYS265 4.2 19.0 1.0
H5'1 B:DUT501 4.2 30.5 0.8
NZ B:LYS303 4.3 20.3 1.0
CA B:CYS265 4.4 16.4 1.0
CA B:CYS263 4.6 17.6 1.0
CA B:CYS252 4.6 17.5 1.0
OG B:SER255 4.6 17.8 1.0
C2' B:DUT501 4.6 26.7 0.8
C5' B:DUT501 4.7 25.4 0.8
C B:CYS263 4.8 17.1 1.0
N1 B:DUT501 4.8 30.4 0.8
CE B:LYS303 4.8 20.4 1.0
OH B:TYR307 4.9 17.4 1.0
N B:THR264 4.9 18.3 1.0
H2'2 B:DUT501 4.9 32.0 0.8
C6 B:DUT501 4.9 33.6 0.8

Reference:

H.Zhang, Y.Zhang. Structural and Biochemical Investigation of Utp Cyclohydrolase To Be Published.
Page generated: Tue Oct 29 19:41:25 2024

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