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Calcium in PDB 5kfc: Human Dna Polymerase Eta-Dna Ternary Complex: Reaction with 1 Mm MN2+ For 180S

Enzymatic activity of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction with 1 Mm MN2+ For 180S

All present enzymatic activity of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction with 1 Mm MN2+ For 180S:
2.7.7.7;

Protein crystallography data

The structure of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction with 1 Mm MN2+ For 180S, PDB code: 5kfc was solved by Y.Gao, W.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.95 / 1.50
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 98.150, 98.150, 82.090, 90.00, 90.00, 120.00
R / Rfree (%) 18 / 21

Other elements in 5kfc:

The structure of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction with 1 Mm MN2+ For 180S also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Human Dna Polymerase Eta-Dna Ternary Complex: Reaction with 1 Mm MN2+ For 180S (pdb code 5kfc). 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 Human Dna Polymerase Eta-Dna Ternary Complex: Reaction with 1 Mm MN2+ For 180S, PDB code: 5kfc:

Calcium binding site 1 out of 1 in 5kfc

Go back to Calcium Binding Sites List in 5kfc
Calcium binding site 1 out of 1 in the Human Dna Polymerase Eta-Dna Ternary Complex: Reaction with 1 Mm MN2+ For 180S


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction with 1 Mm MN2+ For 180S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:11.8
occ:0.25
 MN A:MN503 0.0 11.9 0.8
OD1 A:ASP13 2.2 11.1 0.1
O A:MET14 2.2 11.4 1.0
OD1 A:ASP13 2.2 13.3 0.8
OD2 A:ASP115 2.2 12.0 1.0
O1G A:DTP506 2.2 11.0 1.0
O1B A:DTP506 2.3 10.1 1.0
O1A A:DTP506 2.4 11.1 1.0
CG A:ASP13 3.0 12.8 0.8
OD2 A:ASP13 3.1 14.8 0.8
PB A:DTP506 3.3 10.9 1.0
CG A:ASP115 3.3 9.7 1.0
C A:MET14 3.4 9.3 1.0
CG A:ASP13 3.4 12.8 0.1
PG A:DTP506 3.4 11.0 1.0
PA A:DTP506 3.5 11.5 1.0
MN A:MN501 3.6 13.2 0.8
O3A A:DTP506 3.6 11.7 1.0
OD1 A:ASP115 3.7 12.3 1.0
NZ A:LYS231 3.7 10.2 0.5
O3B A:DTP506 3.8 9.6 1.0
N A:MET14 3.9 9.3 1.0
O A:HOH702 3.9 18.6 1.0
O2G A:DTP506 4.0 10.5 1.0
CA A:MET14 4.1 9.5 1.0
OD2 A:ASP13 4.1 11.2 0.1
C5' A:DTP506 4.1 12.8 1.0
C A:ASP13 4.2 9.5 1.0
O5' A:DTP506 4.3 11.6 1.0
CB A:ASP13 4.3 11.4 0.8
O A:HOH791 4.4 16.0 1.0
N A:ASP15 4.4 7.5 1.0
CB A:ASP13 4.4 11.4 0.1
N A:CYS16 4.5 8.9 1.0
CA A:ASP15 4.6 8.2 1.0
CE A:LYS231 4.6 11.1 0.5
CB A:ASP115 4.6 10.1 1.0
O A:ASP13 4.6 11.3 1.0
CB A:MET14 4.6 10.8 1.0
O2B A:DTP506 4.7 11.5 1.0
O3G A:DTP506 4.7 12.7 1.0
O2A A:DTP506 4.7 13.7 1.0
C A:ASP15 4.7 10.0 1.0
CA A:ASP13 4.8 11.2 0.1
CA A:ASP13 4.8 11.1 0.8
N A:PHE17 4.8 9.5 1.0
O A:ASP115 4.9 12.6 1.0
CB A:PHE17 4.9 7.9 1.0

Reference:

Y.Gao, W.Yang. Capture of A Third MG2+ Is Essential For Catalyzing Dna Synthesis. Science V. 352 1334 2016.
ISSN: ESSN 1095-9203
PubMed: 27284197
DOI: 10.1126/SCIENCE.AAD9633
Page generated: Sat Dec 12 05:33:19 2020

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