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Calcium in PDB 2xhi: Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase

Enzymatic activity of Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase

All present enzymatic activity of Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase:
4.2.99.18;

Protein crystallography data

The structure of Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase, PDB code: 2xhi was solved by B.Dalhus, M.Forsbring, I.H.Helle, E.S.Vik, R.J.Forstrom, P.H.Backe, I.Alseth, M.Bjoras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.63 / 1.55
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 92.669, 92.669, 210.986, 90.00, 90.00, 120.00
R / Rfree (%) 22.935 / 26.472

Calcium Binding Sites:

The binding sites of Calcium atom in the Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase (pdb code 2xhi). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase, PDB code: 2xhi:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2xhi

Go back to Calcium Binding Sites List in 2xhi
Calcium binding site 1 out of 2 in the Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1327

b:58.0
occ:1.00
O A:VAL246 2.5 22.8 1.0
O A:CYS241 2.6 26.9 1.0
O A:LEU243 2.7 23.8 1.0
OP2 C:DC26 3.0 26.3 1.0
OP1 C:DC26 3.4 28.5 1.0
C A:VAL246 3.6 22.4 1.0
C A:LEU243 3.6 24.9 1.0
C A:CYS241 3.6 26.4 1.0
P C:DC26 3.7 26.7 1.0
O C:HOH2022 3.7 42.9 1.0
N A:LEU243 4.1 26.5 1.0
C A:ILE242 4.1 28.2 1.0
O A:ILE242 4.1 28.3 1.0
N A:VAL246 4.1 21.6 1.0
CA A:VAL246 4.3 19.8 1.0
O C:HOH2023 4.3 34.0 1.0
CA A:CYS241 4.4 26.0 1.0
N A:PRO244 4.4 23.2 1.0
CA A:LEU243 4.4 24.4 1.0
N A:GLY247 4.5 21.7 1.0
N A:ILE242 4.5 27.9 1.0
N A:GLY245 4.6 23.7 1.0
CA A:PRO244 4.6 22.3 1.0
CB A:VAL246 4.6 21.6 1.0
CA A:ILE242 4.7 29.9 1.0
O3' C:DT25 4.7 26.8 1.0
CA A:GLY247 4.8 22.6 1.0
CB A:CYS241 4.9 26.9 1.0
C A:PRO244 4.9 25.4 1.0

Calcium binding site 2 out of 2 in 2xhi

Go back to Calcium Binding Sites List in 2xhi
Calcium binding site 2 out of 2 in the Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca1030

b:48.3
occ:1.00
O C:HOH2001 2.5 24.5 1.0
OP2 C:DG24 2.8 16.7 1.0
C8 C:DA22 3.2 22.4 1.0
OD1 A:ASN149 3.2 23.6 1.0
N7 C:DA22 3.5 27.5 1.0
O A:HOH2190 3.6 39.1 1.0
CA A:ASN149 3.7 18.7 1.0
P C:DG24 3.7 15.9 1.0
C2' C:DA22 3.9 22.6 1.0
O C:HOH2010 3.9 39.9 1.0
N9 C:DA22 3.9 21.6 1.0
O C:HOH2007 4.0 36.3 1.0
OP1 C:DG24 4.0 17.4 1.0
O5' C:DG24 4.0 16.0 1.0
O C:HOH2016 4.1 17.4 1.0
CG A:ASN149 4.2 22.8 1.0
C A:ASN149 4.2 19.2 1.0
O C:HOH2018 4.2 31.4 1.0
N A:ASN150 4.3 18.2 1.0
N7 C:DG24 4.4 21.4 1.0
CB A:ASN149 4.4 19.4 1.0
C5 C:DA22 4.5 23.6 1.0
C1' C:DA22 4.5 20.2 1.0
N A:ASN149 4.5 19.6 1.0
C4 C:DA22 4.7 22.0 1.0
C8 C:DG24 4.7 19.5 1.0
C5 C:DG24 4.9 25.2 1.0

Reference:

B.Dalhus, M.Forsbring, I.H.Helle, E.S.Vik, R.J.Forstrom, P.H.Backe, I.Alseth, M.Bjoras. Separation-of-Function Mutants Unravel the Dual- Reaction Mode of Human 8-Oxoguanine Dna Glycosylase. Structure V. 19 117 2011.
ISSN: ISSN 0969-2126
PubMed: 21220122
DOI: 10.1016/J.STR.2010.09.023
Page generated: Fri Jul 12 19:06:18 2024

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