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Zinc in PDB 1zy7: Crystal Structure of the Catalytic Domain of An Adenosine Deaminase That Acts on Rna (HADAR2) Bound to Inositol Hexakisphosphate (Ihp)

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of An Adenosine Deaminase That Acts on Rna (HADAR2) Bound to Inositol Hexakisphosphate (Ihp), PDB code: 1zy7 was solved by M.R.Macbeth, H.L.Schubert, A.P.Vandemark, A.T.Lingam, C.P.Hill, B.L.Bass, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.205, 121.192, 127.331, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 20.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of An Adenosine Deaminase That Acts on Rna (HADAR2) Bound to Inositol Hexakisphosphate (Ihp) (pdb code 1zy7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Catalytic Domain of An Adenosine Deaminase That Acts on Rna (HADAR2) Bound to Inositol Hexakisphosphate (Ihp), PDB code: 1zy7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1zy7

Go back to Zinc Binding Sites List in 1zy7
Zinc binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of An Adenosine Deaminase That Acts on Rna (HADAR2) Bound to Inositol Hexakisphosphate (Ihp)


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 Catalytic Domain of An Adenosine Deaminase That Acts on Rna (HADAR2) Bound to Inositol Hexakisphosphate (Ihp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn801

b:14.2
occ:1.00
O A:HOH1274 2.0 12.5 1.0
ND1 A:HIS394 2.0 12.3 1.0
SG A:CYS451 2.3 12.8 1.0
SG A:CYS516 2.3 11.9 1.0
CE1 A:HIS394 2.9 12.3 1.0
CB A:CYS516 3.1 11.1 1.0
CG A:HIS394 3.1 10.5 1.0
CB A:CYS451 3.3 13.4 1.0
CB A:HIS394 3.5 11.4 1.0
CE A:LYS483 3.6 16.3 1.0
N A:CYS451 3.7 12.7 1.0
O A:HOH949 3.8 18.3 1.0
OE2 A:GLU396 3.8 14.4 1.0
N A:CYS516 3.9 11.1 1.0
NE2 A:HIS394 4.0 12.7 1.0
CA A:CYS451 4.1 12.6 1.0
CA A:CYS516 4.1 10.4 1.0
NZ A:LYS483 4.1 12.5 1.0
CD2 A:HIS394 4.2 11.1 1.0
CD A:GLU396 4.2 15.6 1.0
O A:HOH931 4.3 15.8 1.0
OE1 A:GLU396 4.4 14.7 1.0
O A:HOH1263 4.8 25.5 1.0
C A:CYS451 4.9 12.2 1.0
C A:PRO450 4.9 12.5 1.0
O A:CYS451 4.9 11.2 1.0
CG A:GLU396 4.9 15.4 1.0
CD A:LYS483 5.0 13.2 1.0

Zinc binding site 2 out of 2 in 1zy7

Go back to Zinc Binding Sites List in 1zy7
Zinc binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of An Adenosine Deaminase That Acts on Rna (HADAR2) Bound to Inositol Hexakisphosphate (Ihp)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Catalytic Domain of An Adenosine Deaminase That Acts on Rna (HADAR2) Bound to Inositol Hexakisphosphate (Ihp) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn802

b:15.3
occ:1.00
O B:HOH1166 2.0 16.9 1.0
ND1 B:HIS394 2.1 13.4 1.0
SG B:CYS516 2.3 11.3 1.0
SG B:CYS451 2.3 13.0 1.0
CE1 B:HIS394 3.0 11.8 1.0
CB B:CYS516 3.1 10.6 1.0
CG B:HIS394 3.1 10.2 1.0
CB B:CYS451 3.3 13.0 1.0
CB B:HIS394 3.5 12.4 1.0
CE B:LYS483 3.6 15.9 1.0
N B:CYS451 3.7 11.8 1.0
OE1 B:GLU396 3.7 15.7 1.0
O B:HOH1159 3.8 17.3 1.0
N B:CYS516 3.9 11.2 1.0
NE2 B:HIS394 4.1 12.4 1.0
CA B:CYS451 4.1 11.7 1.0
CD B:GLU396 4.1 15.4 1.0
CA B:CYS516 4.1 11.1 1.0
NZ B:LYS483 4.1 11.5 1.0
CD2 B:HIS394 4.2 13.6 1.0
O B:HOH1153 4.3 17.0 1.0
OE2 B:GLU396 4.3 13.3 1.0
C B:PRO450 4.8 11.6 1.0
C B:CYS451 4.9 12.7 1.0
O B:CYS451 4.9 11.6 1.0
CD B:LYS483 5.0 18.2 1.0
CG B:GLU396 5.0 13.7 1.0
CA B:HIS394 5.0 12.3 1.0

Reference:

M.R.Macbeth, H.L.Schubert, A.P.Vandemark, A.T.Lingam, C.P.Hill, B.L.Bass. Inositol Hexakisphosphate Is Bound in the ADAR2 Core and Required For Rna Editing. Science V. 309 1534 2005.
ISSN: ISSN 0036-8075
PubMed: 16141067
DOI: 10.1126/SCIENCE.1113150
Page generated: Wed Oct 16 21:25:39 2024

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