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Calcium in PDB 1ebm: Crystal Structure of the Human 8-Oxoguanine Glycosylase (HOGG1) Bound to A Substrate Oligonucleotide

Protein crystallography data

The structure of Crystal Structure of the Human 8-Oxoguanine Glycosylase (HOGG1) Bound to A Substrate Oligonucleotide, PDB code: 1ebm was solved by S.D.Bruner, D.P.Norman, G.L.Verdine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.10
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 92.357, 92.357, 212.872, 90.00, 90.00, 120.00
R / Rfree (%) 23.2 / 26.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Human 8-Oxoguanine Glycosylase (HOGG1) Bound to A Substrate Oligonucleotide (pdb code 1ebm). 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 Crystal Structure of the Human 8-Oxoguanine Glycosylase (HOGG1) Bound to A Substrate Oligonucleotide, PDB code: 1ebm:

Calcium binding site 1 out of 1 in 1ebm

Go back to Calcium Binding Sites List in 1ebm
Calcium binding site 1 out of 1 in the Crystal Structure of the Human 8-Oxoguanine Glycosylase (HOGG1) Bound to A Substrate Oligonucleotide


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Human 8-Oxoguanine Glycosylase (HOGG1) Bound to A Substrate Oligonucleotide within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca17

b:66.6
occ:1.00
O C:HOH86 2.3 48.1 1.0
O C:HOH146 2.5 38.1 1.0
O C:HOH63 2.6 43.4 1.0
OP2 C:DA24 3.1 47.1 1.0
C8 C:DA24 4.0 33.1 1.0
N7 C:DA24 4.1 34.0 1.0
N7 C:DG26 4.3 33.5 1.0
ND2 A:ASN149 4.4 31.9 1.0
C2' C:DC23 4.5 52.1 1.0
P C:DA24 4.6 46.6 1.0
O A:HOH381 4.7 32.9 1.0
OP1 C:DG26 4.9 32.0 1.0

Reference:

S.D.Bruner, D.P.Norman, G.L.Verdine. Structural Basis For Recognition and Repair of the Endogenous Mutagen 8-Oxoguanine in Dna. Nature V. 403 859 2000.
ISSN: ISSN 0028-0836
PubMed: 10706276
DOI: 10.1038/35002510
Page generated: Sat Dec 12 02:54:04 2020

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