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Zinc in PDB 4mkp: Crystal Structure of Human Cgas Apo Form

Protein crystallography data

The structure of Crystal Structure of Human Cgas Apo Form, PDB code: 4mkp was solved by K.Kato, R.Ishii, R.Ishitani, O.Nureki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.88 / 1.95
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 123.546, 48.311, 59.565, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 25.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Cgas Apo Form (pdb code 4mkp). 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 Human Cgas Apo Form, PDB code: 4mkp:

Zinc binding site 1 out of 1 in 4mkp

Go back to Zinc Binding Sites List in 4mkp
Zinc binding site 1 out of 1 in the Crystal Structure of Human Cgas Apo Form


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 Human Cgas Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1000

b:26.4
occ:1.00
NE2 A:HIS390 2.2 23.8 1.0
SG A:CYS396 2.3 23.8 1.0
SG A:CYS397 2.4 25.3 1.0
SG A:CYS404 2.5 25.0 1.0
CD2 A:HIS390 2.9 20.7 1.0
CB A:CYS397 3.3 30.5 1.0
CE1 A:HIS390 3.3 27.5 1.0
CB A:CYS404 3.5 19.2 1.0
CB A:CYS396 3.6 29.3 1.0
N A:CYS397 3.6 26.8 1.0
C A:CYS396 3.7 19.9 1.0
N A:CYS404 3.8 21.5 1.0
CA A:CYS397 4.0 29.4 1.0
O A:HOH1148 4.1 26.3 1.0
CA A:CYS404 4.2 21.8 1.0
CA A:CYS396 4.2 22.3 1.0
CG A:HIS390 4.2 21.8 1.0
O A:CYS396 4.2 20.0 1.0
O A:GLU402 4.3 34.5 1.0
NH1 A:ARG406 4.3 22.8 1.0
ND1 A:HIS390 4.3 23.0 1.0
O A:HOH1147 4.5 33.4 1.0
O A:HOH1179 4.6 31.6 1.0
C A:CYS404 4.7 28.7 1.0
O A:CYS404 4.7 23.5 1.0
O A:HOH1187 4.9 28.6 1.0
C A:LYS403 5.0 33.5 1.0

Reference:

K.Kato, R.Ishii, E.Goto, R.Ishitani, F.Tokunaga, O.Nureki. Structural and Functional Analyses of Dna-Sensing and Immune Activation By Human Cgas Plos One V. 8 76983 2013.
ISSN: ESSN 1932-6203
PubMed: 24116191
DOI: 10.1371/JOURNAL.PONE.0076983
Page generated: Wed Dec 16 05:35:32 2020

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