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Iron in PDB 8iil: Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G

Enzymatic activity of Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G

All present enzymatic activity of Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G:
3.2.2.27;

Protein crystallography data

The structure of Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G, PDB code: 8iil was solved by S.Aroli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.85 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 36.78, 50.83, 55.42, 90, 105.08, 90
R / Rfree (%) 19.1 / 23.7

Iron Binding Sites:

The binding sites of Iron atom in the Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G (pdb code 8iil). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G, PDB code: 8iil:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 8iil

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Iron binding site 1 out of 4 in the Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:15.4
occ:1.00
FE1 A:SF4301 0.0 15.4 1.0
S3 A:SF4301 2.3 10.9 1.0
S2 A:SF4301 2.3 11.0 1.0
S4 A:SF4301 2.3 12.7 1.0
SG A:CYS120 2.5 14.1 1.0
FE4 A:SF4301 2.8 19.5 1.0
FE3 A:SF4301 2.8 18.2 1.0
FE2 A:SF4301 2.8 16.7 1.0
CB A:CYS120 3.3 11.7 1.0
CA A:CYS120 3.8 15.1 1.0
N A:LYS94 3.9 15.7 1.0
S1 A:SF4301 4.0 16.5 1.0
CD1 A:TRP123 4.2 15.1 1.0
CB A:LYS94 4.3 15.3 1.0
CG A:LYS94 4.4 17.5 1.0
NE1 A:TRP123 4.5 15.4 1.0
N A:CYS120 4.6 14.4 1.0
CA A:LYS94 4.7 16.2 1.0
SG A:CYS24 4.8 16.4 1.0
SG A:CYS27 4.8 15.1 1.0
CA A:VAL93 4.8 13.8 1.0
C A:VAL93 4.8 17.0 1.0
N A:HIS95 4.9 14.4 1.0
ND1 A:HIS95 5.0 16.1 1.0

Iron binding site 2 out of 4 in 8iil

Go back to Iron Binding Sites List in 8iil
Iron binding site 2 out of 4 in the Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:16.7
occ:1.00
FE2 A:SF4301 0.0 16.7 1.0
SG A:CYS27 2.3 15.1 1.0
S4 A:SF4301 2.3 12.7 1.0
S1 A:SF4301 2.3 16.5 1.0
S3 A:SF4301 2.3 10.9 1.0
FE3 A:SF4301 2.8 18.2 1.0
FE4 A:SF4301 2.8 19.5 1.0
FE1 A:SF4301 2.8 15.4 1.0
N A:CYS27 3.3 16.9 1.0
CB A:CYS27 3.4 15.5 1.0
CA A:CYS27 3.8 17.4 1.0
S2 A:SF4301 4.0 11.0 1.0
O A:CYS27 4.1 19.2 1.0
C A:CYS27 4.2 19.3 1.0
C A:GLY26 4.2 18.2 1.0
CA A:GLY26 4.5 17.9 1.0
N A:GLY26 4.6 19.1 1.0
CB A:LEU29 4.7 16.2 1.0
N A:LEU29 4.8 16.7 1.0
ND1 A:HIS95 5.0 16.1 1.0
N A:GLY28 5.0 17.7 1.0

Iron binding site 3 out of 4 in 8iil

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Iron binding site 3 out of 4 in the Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:18.2
occ:1.00
FE3 A:SF4301 0.0 18.2 1.0
S1 A:SF4301 2.3 16.5 1.0
S4 A:SF4301 2.3 12.7 1.0
S2 A:SF4301 2.3 11.0 1.0
SG A:CYS24 2.3 16.4 1.0
FE4 A:SF4301 2.8 19.5 1.0
FE2 A:SF4301 2.8 16.7 1.0
FE1 A:SF4301 2.8 15.4 1.0
CB A:CYS24 3.3 17.5 1.0
N A:GLY26 3.5 19.1 1.0
CA A:GLY26 3.9 17.9 1.0
S3 A:SF4301 3.9 10.9 1.0
NE1 A:TRP123 4.0 15.4 1.0
C A:CYS24 4.1 20.8 1.0
O A:CYS24 4.2 19.0 1.0
N A:CYS27 4.3 16.9 1.0
CA A:CYS24 4.3 20.6 1.0
CB A:ALA4 4.3 17.1 1.0
N A:ARG25 4.3 20.4 1.0
C A:ARG25 4.5 22.1 1.0
C A:GLY26 4.5 18.2 1.0
CD1 A:TRP123 4.6 15.1 1.0
ND1 A:HIS95 4.7 16.1 1.0
CA A:ARG25 4.8 20.5 1.0
SG A:CYS27 5.0 15.1 1.0

Iron binding site 4 out of 4 in 8iil

Go back to Iron Binding Sites List in 8iil
Iron binding site 4 out of 4 in the Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Complex Form of Msmudgx H109G Mutant and Uracil- Obtained From Uracil Dna (Ttutt) Post Its Cleavage By Msmudgx H109G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:19.5
occ:1.00
FE4 A:SF4301 0.0 19.5 1.0
S2 A:SF4301 2.3 11.0 1.0
S3 A:SF4301 2.3 10.9 1.0
S1 A:SF4301 2.3 16.5 1.0
ND1 A:HIS95 2.3 16.1 1.0
FE3 A:SF4301 2.8 18.2 1.0
FE1 A:SF4301 2.8 15.4 1.0
FE2 A:SF4301 2.8 16.7 1.0
CG A:HIS95 3.2 15.9 1.0
CE1 A:HIS95 3.3 14.9 1.0
CB A:HIS95 3.4 11.5 1.0
S4 A:SF4301 3.9 12.7 1.0
N A:HIS95 4.0 14.4 1.0
CA A:HIS95 4.4 13.7 1.0
CD2 A:HIS95 4.4 15.2 1.0
NE2 A:HIS95 4.4 12.7 1.0
N A:TYR30 4.6 18.4 1.0
C A:LYS94 4.6 14.0 1.0
CB A:LYS94 4.7 15.3 1.0
CB A:TYR30 4.7 19.4 1.0
SG A:CYS27 4.7 15.1 1.0
N A:LYS94 4.8 15.7 1.0
SG A:CYS24 4.8 16.4 1.0
CA A:TYR30 4.9 19.6 1.0
CA A:LYS94 4.9 16.2 1.0
O A:CYS24 4.9 19.0 1.0
CB A:CYS24 5.0 17.5 1.0

Reference:

S.Aroli, E.J.Woo, B.Gopal, U.Varshney. Mutational and Structural Analyses of Udgx: Insights Into the Active Site Pocket Architecture and Its Evolution. Nucleic Acids Res. 2023.
ISSN: ESSN 1362-4962
PubMed: 37283083
DOI: 10.1093/NAR/GKAD486
Page generated: Thu Aug 7 18:09:14 2025

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