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Calcium in PDB 1n3c: Structural and Biochemical Exploration of A Critical Amino Acid in Human 8-Oxoguanine Glycosylase

Protein crystallography data

The structure of Structural and Biochemical Exploration of A Critical Amino Acid in Human 8-Oxoguanine Glycosylase, PDB code: 1n3c was solved by D.P.Norman, S.J.Chung, G.L.Verdine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.03 / 2.70
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 92.255, 92.255, 210.600, 90.00, 90.00, 120.00
R / Rfree (%) 22.5 / 27.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Structural and Biochemical Exploration of A Critical Amino Acid in Human 8-Oxoguanine Glycosylase (pdb code 1n3c). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structural and Biochemical Exploration of A Critical Amino Acid in Human 8-Oxoguanine Glycosylase, PDB code: 1n3c:

Calcium binding site 1 out of 1 in 1n3c

Go back to Calcium Binding Sites List in 1n3c
Calcium binding site 1 out of 1 in the Structural and Biochemical Exploration of A Critical Amino Acid in Human 8-Oxoguanine Glycosylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structural and Biochemical Exploration of A Critical Amino Acid in Human 8-Oxoguanine Glycosylase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca1001

b:0.9
occ:1.00
O A:HOH341 2.7 40.0 1.0
O C:HOH1004 2.8 38.1 1.0
N7 C:DA22 3.5 45.9 1.0
ND2 A:ASN149 3.8 41.1 1.0
O6 C:DG24 4.0 43.8 1.0
C8 C:DA22 4.0 45.0 1.0
N7 C:DG24 4.3 44.9 1.0
OP2 C:DA22 4.4 66.2 1.0
C6 C:DG24 4.6 43.3 1.0
C2' C:DC21 4.7 71.4 1.0
C5 C:DG24 4.7 44.3 1.0
C5 C:DA22 4.8 43.9 1.0
CG A:ASN149 4.9 42.2 1.0

Reference:

D.P.Norman, S.J.Chung, G.L.Verdine. Structural and Biochemical Exploration of A Critical Amino Acid in Human 8-Oxoguanine Glycosylase Biochemistry V. 42 1564 2003.
ISSN: ISSN 0006-2960
PubMed: 12578369
DOI: 10.1021/BI026823D
Page generated: Sat Dec 12 03:07:57 2020

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