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Zinc in PDB 6edc: Hcgas-16BP Dsdna Complex

Enzymatic activity of Hcgas-16BP Dsdna Complex

All present enzymatic activity of Hcgas-16BP Dsdna Complex:
2.7.7.86;

Protein crystallography data

The structure of Hcgas-16BP Dsdna Complex, PDB code: 6edc was solved by W.Xie, L.Lama, C.Adura, J.F.Glickman, T.Tuschl, D.J.Patel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 86.44 / 2.71
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 99.813, 99.813, 238.644, 90.00, 90.00, 120.00
R / Rfree (%) 23.9 / 27.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Hcgas-16BP Dsdna Complex (pdb code 6edc). 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 Hcgas-16BP Dsdna Complex, PDB code: 6edc:

Zinc binding site 1 out of 1 in 6edc

Go back to Zinc Binding Sites List in 6edc
Zinc binding site 1 out of 1 in the Hcgas-16BP Dsdna Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Hcgas-16BP Dsdna Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:81.2
occ:1.00
NE2 A:HIS390 2.0 39.9 1.0
SG A:CYS404 2.2 61.8 1.0
SG A:CYS397 2.3 64.2 1.0
SG A:CYS396 2.3 62.6 1.0
CB A:CYS404 2.8 48.8 1.0
CD2 A:HIS390 2.9 54.6 1.0
CE1 A:HIS390 3.1 63.2 1.0
N A:CYS404 3.4 59.4 1.0
CB A:CYS397 3.5 54.5 1.0
CA A:CYS404 3.6 55.5 1.0
N A:CYS397 3.6 71.5 1.0
CB A:CYS396 3.7 54.5 1.0
C A:CYS396 3.9 57.2 1.0
O A:GLU402 3.9 71.1 1.0
CA A:CYS397 4.1 66.5 1.0
CG A:HIS390 4.1 42.7 1.0
ND1 A:HIS390 4.1 47.0 1.0
CA A:CYS396 4.2 49.6 1.0
C A:CYS404 4.3 58.7 1.0
O A:CYS396 4.4 52.0 1.0
NH2 A:ARG406 4.4 46.7 1.0
C A:LYS403 4.5 69.4 1.0
O A:CYS404 4.5 69.2 1.0
CA A:LYS403 4.9 74.3 1.0

Reference:

W.Xie, L.Lama, C.Adura, D.Tomita, J.F.Glickman, T.Tuschl, D.J.Patel. Human Cgas Catalytic Domain Has An Additional Dna-Binding Interface That Enhances Enzymatic Activity and Liquid-Phase Condensation. Proc.Natl.Acad.Sci.Usa V. 116 11946 2019.
ISSN: ESSN 1091-6490
PubMed: 31142647
DOI: 10.1073/PNAS.1905013116
Page generated: Mon Oct 28 20:04:23 2024

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