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Zinc in PDB 3f2d: Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn

Enzymatic activity of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn

All present enzymatic activity of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn:
2.7.7.7;

Protein crystallography data

The structure of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn, PDB code: 3f2d was solved by D.R.Davies, R.J.Evans, J.M.Bullard, J.Christensen, L.S.Green, J.W.Guiles, W.K.Ribble, N.Janjic, T.C.Jarvis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.15 / 2.51
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 115.997, 139.479, 184.074, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 25.4

Other elements in 3f2d:

The structure of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn also contains other interesting chemical elements:

Manganese (Mn) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn (pdb code 3f2d). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn, PDB code: 3f2d:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3f2d

Go back to Zinc Binding Sites List in 3f2d
Zinc binding site 1 out of 2 in the Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn4

b:79.9
occ:1.00
SG A:CYS947 2.0 50.9 1.0
SG A:CYS944 2.1 39.0 1.0
CB A:CYS922 2.4 42.8 1.0
SG A:CYS922 2.5 44.5 1.0
SG A:CYS919 2.7 45.3 1.0
CB A:CYS944 3.0 44.1 1.0
CB A:CYS947 3.0 49.0 1.0
CB A:CYS919 3.1 43.2 1.0
CA A:CYS922 3.4 43.1 1.0
N A:CYS922 3.4 43.1 1.0
OG1 A:THR949 3.6 50.0 1.0
N A:CYS947 3.8 48.7 1.0
CA A:CYS947 4.0 48.9 1.0
C A:CYS922 4.0 43.0 1.0
N A:LYS923 4.3 43.0 1.0
CA A:CYS944 4.4 44.2 1.0
CA A:CYS919 4.6 43.7 1.0
CB A:THR949 4.6 48.6 1.0
C A:ASN921 4.7 43.1 1.0
OD1 A:ASN921 4.7 41.5 1.0
CB A:ARG946 4.7 48.9 1.0
C A:ARG946 4.8 48.7 1.0
N A:HIS924 4.8 42.3 1.0
C A:CYS947 4.8 48.7 1.0
CB A:HIS924 4.8 42.4 1.0
O A:CYS922 4.8 43.1 1.0
CB A:ASN921 4.9 42.8 1.0
N A:GLY948 4.9 48.6 1.0
O A:CYS944 5.0 45.3 1.0
C A:CYS944 5.0 45.2 1.0

Zinc binding site 2 out of 2 in 3f2d

Go back to Zinc Binding Sites List in 3f2d
Zinc binding site 2 out of 2 in the Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mn and Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn5

b:53.7
occ:1.00
OD1 A:ASP355 1.9 47.1 1.0
NE2 A:HIS380 2.1 51.2 1.0
NE2 A:HIS745 2.1 44.8 1.0
O4 A:PO46 2.4 68.2 1.0
CE1 A:HIS380 2.9 50.8 1.0
CG A:ASP355 3.0 46.1 1.0
CD2 A:HIS745 3.1 48.0 1.0
CE1 A:HIS745 3.1 48.3 1.0
CD2 A:HIS380 3.2 49.2 1.0
O1 A:PO46 3.3 69.3 1.0
P A:PO46 3.3 69.6 1.0
OD2 A:ASP355 3.4 48.5 1.0
CE1 A:HIS348 3.9 47.1 1.0
NE2 A:HIS348 4.0 47.0 1.0
ND1 A:HIS380 4.0 50.0 1.0
ND1 A:HIS348 4.1 47.8 1.0
CG A:HIS380 4.2 48.1 1.0
ND1 A:HIS745 4.2 47.8 1.0
O2 A:PO46 4.2 70.1 1.0
CG A:HIS745 4.3 49.8 1.0
CD2 A:HIS348 4.3 44.7 1.0
CB A:ASP355 4.3 45.2 1.0
CG A:HIS348 4.3 45.2 1.0
NH1 A:ARG755 4.4 54.5 1.0
O3 A:PO46 4.4 70.1 1.0
MN A:MN3 4.7 36.9 1.0
OE1 A:GLU405 4.7 45.9 1.0

Reference:

R.J.Evans, D.R.Davies, J.M.Bullard, J.Christensen, L.S.Green, J.W.Guiles, J.D.Pata, W.K.Ribble, N.Janjic, T.C.Jarvis. Structure of Polc Reveals Unique Dna Binding and Fidelity Determinants. Proc.Natl.Acad.Sci.Usa V. 105 20695 2008.
ISSN: ISSN 0027-8424
PubMed: 19106298
DOI: 10.1073/PNAS.0809989106
Page generated: Thu Oct 24 13:02:55 2024

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