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Zinc in PDB 3t9h: Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2

Protein crystallography data

The structure of Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2, PDB code: 3t9h was solved by A.H.Ahmed, S.Wang, H.H.Chuang, R.E.Oswald, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.37 / 2.02
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.841, 113.918, 164.786, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 23.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 (pdb code 3t9h). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2, PDB code: 3t9h:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in 3t9h

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Zinc binding site 1 out of 5 in the Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1

b:40.1
occ:1.00
NE2 B:HIS23 2.4 40.1 1.0
CD2 B:HIS23 3.1 38.7 1.0
CE1 B:HIS23 3.5 37.1 1.0
CG B:HIS23 4.4 35.3 1.0
ND1 B:HIS23 4.5 35.0 1.0
CB B:MET19 4.5 36.2 1.0
CG B:MET19 4.7 36.1 1.0

Zinc binding site 2 out of 5 in 3t9h

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Zinc binding site 2 out of 5 in the Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2

b:31.9
occ:1.00
NE2 B:HIS46 2.2 34.8 1.0
OE1 F:GLU166 2.3 29.9 1.0
OE2 F:GLU166 2.4 33.4 1.0
CD F:GLU166 2.7 32.8 1.0
NZ B:LYS45 2.7 44.2 1.0
OE1 B:GLU42 2.9 32.7 1.0
CE1 B:HIS46 3.0 40.2 1.0
CD2 B:HIS46 3.3 33.4 1.0
CD B:GLU42 3.7 37.2 1.0
OE2 B:GLU42 3.8 32.3 1.0
CE B:LYS45 4.1 43.0 1.0
CG F:GLU166 4.2 31.3 1.0
ND1 B:HIS46 4.2 34.3 1.0
O F:ALA165 4.2 29.1 1.0
CG B:HIS46 4.4 33.6 1.0
CD B:LYS45 4.4 44.2 1.0
N F:SER168 4.5 31.8 1.0
CB F:SER168 4.6 29.8 1.0
O F:HOH313 4.7 39.5 1.0
CA F:SER168 4.8 29.4 1.0
CD2 B:LEU241 4.8 31.6 1.0
CB F:GLU166 5.0 31.7 1.0

Zinc binding site 3 out of 5 in 3t9h

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Zinc binding site 3 out of 5 in the Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn3

b:38.2
occ:1.00
CD D:GLU24 2.3 49.5 1.0
CG D:GLU24 2.6 47.7 1.0
NE2 D:HIS23 2.6 41.5 1.0
OE1 D:GLU24 2.6 54.6 1.0
OE2 D:GLU24 2.9 39.6 1.0
CD2 D:HIS23 3.1 41.0 1.0
CE1 D:HIS23 3.8 39.8 1.0
CB D:GLU24 4.1 48.7 1.0
CG D:HIS23 4.4 43.4 1.0
O D:HOH563 4.5 55.1 1.0
O D:HOH438 4.6 49.1 1.0
ND1 D:HIS23 4.7 39.7 1.0
CA D:GLU24 4.9 49.9 1.0

Zinc binding site 4 out of 5 in 3t9h

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Zinc binding site 4 out of 5 in the Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn262

b:65.9
occ:1.00
NE2 D:HIS46 2.3 55.3 1.0
OE1 D:GLU42 2.4 46.4 1.0
CD2 D:HIS46 3.2 47.2 1.0
CD D:GLU42 3.3 47.8 1.0
CE1 D:HIS46 3.3 55.8 1.0
OE2 D:GLU42 3.6 55.3 1.0
CD2 D:LEU241 4.0 37.8 1.0
NZ D:LYS45 4.1 64.2 1.0
NE2 D:GLN244 4.2 50.0 1.0
CG D:HIS46 4.4 48.0 1.0
CD D:LYS45 4.4 49.5 1.0
ND1 D:HIS46 4.4 50.5 1.0
CG D:GLU42 4.6 39.1 1.0
CD2 D:LEU246 4.7 44.6 1.0
CB D:GLU42 4.9 36.4 1.0
CE D:LYS45 4.9 57.2 1.0

Zinc binding site 5 out of 5 in 3t9h

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Zinc binding site 5 out of 5 in the Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Kainate Bound to A Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn262

b:38.4
occ:1.00
NE2 F:HIS46 2.3 33.1 1.0
OE1 F:GLU42 2.5 33.2 1.0
CE1 F:HIS46 3.1 37.5 1.0
NE2 F:GLN244 3.2 42.5 1.0
CD F:GLU42 3.2 32.5 1.0
OE2 F:GLU42 3.3 36.2 1.0
CD2 F:HIS46 3.4 32.7 1.0
CD2 F:LEU241 3.5 31.7 1.0
NZ F:LYS45 4.1 35.0 1.0
CD F:GLN244 4.1 44.5 1.0
OE1 F:GLN244 4.3 48.1 1.0
ND1 F:HIS46 4.3 32.9 1.0
CG F:HIS46 4.5 31.4 1.0
CG F:GLU42 4.5 33.1 1.0
CE F:LYS45 4.8 40.5 1.0
O F:HOH519 4.8 42.9 1.0

Reference:

A.H.Ahmed, S.Wang, H.H.Chuang, R.E.Oswald. Mechanism of Ampa Receptor Activation By Partial Agonists: Disulfide Trapping of Closed Lobe Conformations. J.Biol.Chem. V. 286 35257 2011.
ISSN: ISSN 0021-9258
PubMed: 21846932
DOI: 10.1074/JBC.M111.269001
Page generated: Wed Dec 16 04:51:53 2020

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