Zinc in PDB 9f28: Crystal Structure of the Heterodimeric Primase From Pyrococcus Abyssi (Deletion of the Pril-Ctd Domain)

Protein crystallography data

The structure of Crystal Structure of the Heterodimeric Primase From Pyrococcus Abyssi (Deletion of the Pril-Ctd Domain), PDB code: 9f28 was solved by C.Madru, L.Sauguet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.51 / 1.85
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 116.574, 116.574, 121.084, 90, 90, 90
R / Rfree (%) 19.9 / 22.4

Other elements in 9f28:

The structure of Crystal Structure of the Heterodimeric Primase From Pyrococcus Abyssi (Deletion of the Pril-Ctd Domain) also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Heterodimeric Primase From Pyrococcus Abyssi (Deletion of the Pril-Ctd Domain) (pdb code 9f28). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Heterodimeric Primase From Pyrococcus Abyssi (Deletion of the Pril-Ctd Domain), PDB code: 9f28:

Zinc binding site 1 out of 1 in 9f28

Go back to Zinc Binding Sites List in 9f28
Zinc binding site 1 out of 1 in the Crystal Structure of the Heterodimeric Primase From Pyrococcus Abyssi (Deletion of the Pril-Ctd Domain)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Heterodimeric Primase From Pyrococcus Abyssi (Deletion of the Pril-Ctd Domain) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:42.0
occ:1.00
CE1 A:HIS108 2.0 71.9 1.0
SG A:CYS106 2.3 46.2 1.0
SG A:CYS114 2.4 40.7 1.0
SG A:CYS117 2.4 37.2 1.0
NE2 A:HIS108 2.5 71.7 1.0
ND1 A:HIS108 3.2 71.2 1.0
CB A:CYS117 3.3 32.7 1.0
CB A:CYS114 3.3 39.2 1.0
CB A:CYS106 3.4 54.3 1.0
N A:CYS114 3.5 40.8 1.0
N A:CYS117 3.5 31.1 1.0
CD2 A:HIS108 3.8 70.4 1.0
CA A:CYS114 3.8 39.0 1.0
CA A:CYS117 4.0 31.2 1.0
CG A:HIS108 4.1 69.4 1.0
O A:CYS114 4.2 36.6 1.0
C A:VAL113 4.2 43.6 1.0
C A:CYS114 4.3 36.9 1.0
O A:HOH760 4.5 50.9 1.0
CA A:VAL113 4.6 46.5 1.0
C A:ILE116 4.7 32.0 1.0
NH2 A:ARG104 4.7 62.0 1.0
CB A:ILE116 4.7 34.6 1.0
CD A:ARG104 4.7 60.1 1.0
CA A:CYS106 4.8 57.0 1.0
N A:ILE116 4.8 33.1 1.0
CA A:ILE116 4.9 33.3 1.0

Reference:

M.Martinez-Carranza, L.Vialle, C.Madru, F.Cordier, A.Diskirici Tekpinar, A.Haouz, P.Legrand, R.A.Le Meur, P.England, R.Dulermo, I.Guijarro, G.Henneke, L.Sauguet. Communication Between Dna Polymerases and Replication Protein A Within the Archaeal Replisome To Be Published.
Page generated: Tue Dec 10 21:56:07 2024

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