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Zinc in PDB 3t9u: Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2

Protein crystallography data

The structure of Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2, PDB code: 3t9u was solved by A.H.Ahmed, R.E.Oswald, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.50 / 1.97
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 114.724, 165.243, 47.651, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 21.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 (pdb code 3t9u). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2, PDB code: 3t9u:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in 3t9u

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Zinc binding site 1 out of 5 in the Cnqx Bound to An Oxidized 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 Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:27.7
occ:1.00
NE2 A:HIS23 2.2 21.8 1.0
CE1 A:HIS23 3.1 26.9 1.0
CD2 A:HIS23 3.3 19.2 1.0
ND1 A:HIS23 4.3 21.1 1.0
CG A:HIS23 4.4 19.1 1.0
CB A:MET19 5.0 19.0 1.0

Zinc binding site 2 out of 5 in 3t9u

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Zinc binding site 2 out of 5 in the Cnqx Bound to An Oxidized 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 Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn3

b:21.9
occ:1.00
OE1 B:GLU24 2.4 30.3 1.0
CD B:GLU24 2.4 29.9 1.0
OE2 B:GLU24 2.5 29.3 1.0
NE2 B:HIS23 2.5 23.9 1.0
CD2 B:HIS23 3.3 23.3 1.0
CG B:GLU24 3.4 30.3 1.0
CE1 B:HIS23 3.6 24.1 1.0
CG B:HIS23 4.5 24.3 1.0
ND1 B:HIS23 4.6 19.9 1.0
CB B:GLU24 4.8 30.6 1.0

Zinc binding site 3 out of 5 in 3t9u

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Zinc binding site 3 out of 5 in the Cnqx Bound to An Oxidized 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 Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn262

b:71.4
occ:1.00
OE1 B:GLU42 2.3 37.0 1.0
NE2 B:HIS46 2.5 46.7 1.0
CD2 B:HIS46 3.4 43.2 1.0
CD B:GLU42 3.5 35.0 1.0
CE1 B:HIS46 3.5 48.1 1.0
OE2 B:GLU42 4.0 42.5 1.0
CD2 B:LEU241 4.1 25.0 1.0
OE1 B:GLN244 4.3 44.9 1.0
NZ B:LYS45 4.5 51.9 1.0
CD B:LYS45 4.6 45.0 1.0
CG B:HIS46 4.6 42.3 1.0
ND1 B:HIS46 4.6 44.6 1.0
CG B:GLU42 4.6 27.6 1.0
CB B:GLU42 4.8 23.7 1.0
CE B:LYS45 5.0 48.6 1.0

Zinc binding site 4 out of 5 in 3t9u

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Zinc binding site 4 out of 5 in the Cnqx Bound to An Oxidized 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 Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn2

b:18.1
occ:1.00
OE1 C:GLU166 1.7 15.2 1.0
OE1 A:GLU42 2.0 17.8 1.0
NE2 A:HIS46 2.1 21.4 1.0
CD C:GLU166 2.5 22.4 1.0
OE2 C:GLU166 2.7 19.3 1.0
CD A:GLU42 2.9 19.2 1.0
CD2 A:HIS46 3.0 19.0 1.0
CE1 A:HIS46 3.1 25.1 1.0
OE2 A:GLU42 3.2 17.0 1.0
CG C:GLU166 4.0 17.0 1.0
CG A:HIS46 4.1 21.2 1.0
ND1 A:HIS46 4.2 20.2 1.0
CD2 A:LEU241 4.2 20.1 1.0
CG A:GLU42 4.3 14.1 1.0
N C:SER168 4.4 14.3 1.0
CB A:GLU42 4.6 11.7 1.0
CB C:GLU166 4.7 18.3 1.0
O C:ALA165 4.8 15.9 1.0
CB C:SER168 4.8 12.1 1.0
CD A:LYS45 4.8 35.2 1.0
CE A:LYS45 4.9 36.9 1.0
CA C:SER168 4.9 13.0 1.0
CA C:PRO167 5.0 17.3 1.0
CA C:GLU166 5.0 17.0 1.0

Zinc binding site 5 out of 5 in 3t9u

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Zinc binding site 5 out of 5 in the Cnqx Bound to An Oxidized 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 Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn262

b:18.3
occ:1.00
NE2 C:HIS46 1.9 10.8 1.0
OE1 C:GLU42 2.0 18.9 1.0
CD2 C:HIS46 2.8 16.6 1.0
CE1 C:HIS46 2.9 21.1 1.0
CD C:GLU42 2.9 17.2 1.0
OE2 C:GLU42 3.3 20.8 1.0
OE1 C:GLN244 3.6 29.7 1.0
CE C:LYS45 3.8 25.4 1.0
CD2 C:LEU241 3.8 15.6 1.0
CG C:HIS46 4.0 15.3 1.0
ND1 C:HIS46 4.0 20.1 1.0
NZ C:LYS45 4.0 21.0 1.0
CG C:GLU42 4.3 11.5 1.0
NE2 C:GLN244 4.4 28.0 1.0
CD C:GLN244 4.4 28.3 1.0
CD1 C:LEU246 4.6 26.7 1.0
CB C:GLU42 4.6 10.4 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: Sat Oct 26 16:26:16 2024

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