Glutamate receptor 2

Peptide B accession

Peptide A residue number

330

Peptide B residue number

Ligandability

Cysteine 330 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 75 of Glutamate receptor 1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 78 of Glutamate receptor 2 and cysteine 334 of Glutamate receptor 3 (57 and 312 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of the ampa receptor glua2/a3 n-terminal domain heterodimer

Structure deposition date

2016-02-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 3

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

334

Ligandability

Cysteine 78 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 334 of Glutamate receptor 3

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 78 of Glutamate receptor 2 and cysteine 331 of Glutamate receptor 4 (57 and 310 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer

Structure deposition date

2016-02-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 4

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

331

Ligandability

Cysteine 78 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 331 of Glutamate receptor 4

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 330 of Glutamate receptor 2 and cysteine 334 of Glutamate receptor 3 (309 and 312 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of the ampa receptor glua2/a3 n-terminal domain heterodimer

Structure deposition date

2016-02-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 3

Peptide A accession

Peptide B accession

Peptide A residue number

330

Peptide B residue number

334

Ligandability

Cysteine 330 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 334 of Glutamate receptor 3

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 78 of Glutamate receptor 2 and cysteine 84 of Glutamate receptor 4 (57 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer

Structure deposition date

2016-02-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 4

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 78 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 84 of Glutamate receptor 4

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 75 of Glutamate receptor 1 and cysteine 78 of Glutamate receptor 2 (57 and 57 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6njl

Structure name

architecture and subunit arrangement of native ampa receptors

Structure deposition date

2019-01-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor 2

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 75 of Glutamate receptor 1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 78 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Glutamate receptor 2 at cysteines 78 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2wjx

Structure name

crystal structure of the human ionotropic glutamate receptor glur2 atd region at 4

Structure deposition date

2009-06-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 2

Peptide A accession

P42262

Peptide B accession

P42262

Peptide A residue number

Peptide B residue number

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 330 of Glutamate receptor 2 and cysteine 331 of Glutamate receptor 4 (309 and 310 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer

Structure deposition date

2016-02-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 4

Peptide A accession

Peptide B accession

Peptide A residue number

330

Peptide B residue number

331

Ligandability

Cysteine 330 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 331 of Glutamate receptor 4

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 78 of Glutamate receptor 2 and cysteine 85 of Glutamate receptor 3 (57 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of the ampa receptor glua2/a3 n-terminal domain heterodimer

Structure deposition date

2016-02-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 3

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 78 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 85 of Glutamate receptor 3

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 549 of Glutamate receptor 2 and cysteine 9 of Protein cornichon homolog 2 (528 and 9 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7oca

Structure name

resting state full-length glua1/a2 heterotertramer in complex with tarp gamma 8 and cnih2

Structure deposition date

2021-04-26

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Glutamate receptor 2

Peptide B name

Protein cornichon homolog 2

Peptide A accession

Peptide B accession

Q5BJU5

Peptide A residue number

549

Peptide B residue number

Ligandability

Cysteine 549 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 9 of Protein cornichon homolog 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Glutamate receptor 2 at cysteines 330 and 330 (313 and 313 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4u1w

Structure name

full length glua2-kainate-(r,r)-2b complex crystal form a

Structure deposition date

2014-07-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 2

Peptide A accession

Peptide B accession

Peptide A residue number

330

Peptide B residue number

330

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Glutamate receptor 2 at cysteines 78 and 330 (61 and 313 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4u1w

Structure name

full length glua2-kainate-(r,r)-2b complex crystal form a

Structure deposition date

2014-07-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 2

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

330

Ligandability

Cysteine 78 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 330 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 323 of Glutamate receptor 1 and cysteine 330 of Glutamate receptor 2 (305 and 309 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6njl

Structure name

architecture and subunit arrangement of native ampa receptors

Structure deposition date

2019-01-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor 2

Peptide A accession

Peptide B accession

Peptide A residue number

323

Peptide B residue number

330

Ligandability

Cysteine 323 of Glutamate receptor 1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 330 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 330 of Glutamate receptor 2 and cysteine 85 of Glutamate receptor 3 (309 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of the ampa receptor glua2/a3 n-terminal domain heterodimer

Structure deposition date

2016-02-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 3

Peptide A accession

Peptide B accession

Peptide A residue number

330

Peptide B residue number

Ligandability

Cysteine 330 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 85 of Glutamate receptor 3

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 323 of Glutamate receptor 1 and cysteine 78 of Glutamate receptor 2 (305 and 57 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6njn

Structure name

architecture and subunit arrangement of native ampa receptors

Structure deposition date

2019-01-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor 2

Peptide A accession

Peptide B accession

Peptide A residue number

323

Peptide B residue number

Ligandability

Cysteine 323 of Glutamate receptor 1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 78 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 330 of Glutamate receptor 2 and cysteine 84 of Glutamate receptor 4 (309 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer

Structure deposition date

2016-02-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 4

Peptide A accession

Peptide B accession

Peptide A residue number

330

Peptide B residue number

Ligandability

Cysteine 330 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 84 of Glutamate receptor 4

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Glutamate receptor 2 at cysteines 610 and 610 (589 and 589 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7rz5

Structure name

structure of the complex of lbd-tmd part of ampa receptor glua2 with auxiliary subunit tarp gamma-5 bound to competitive antagonist zk 200775

Structure deposition date

2021-08-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 2

Peptide A accession

Peptide B accession

Peptide A residue number

610

Peptide B residue number

610

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 603 of Glutamate receptor 1 and cysteine 610 of Glutamate receptor 2 (585 and 589 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7ocd

Structure name

resting state glua1/a2 heterotetramer in complex with auxiliary subunit tarp gamma 8 (lbd-tmd)

Structure deposition date

2021-04-26

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor 2

Peptide A accession

Peptide B accession

Peptide A residue number

603

Peptide B residue number

610

Ligandability

Cysteine 603 of Glutamate receptor 1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 610 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 549 of Glutamate receptor 2 and cysteine 9 of Protein cornichon homolog 3 (528 and 9 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6ucb

Structure name

glua2 in complex with its auxiliary subunit cnih3 - with antagonist zk200775, lbd, tmd, cnih3, and lipids

Structure deposition date

2019-09-15

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Glutamate receptor 2

Peptide B name

Protein cornichon homolog 3

Peptide A accession

Peptide B accession

Q6ZWS4

Peptide A residue number

549

Peptide B residue number

Ligandability

Cysteine 549 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 9 of Protein cornichon homolog 3

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 739 and 794 (206 and 261 respectively in this structure).

Details

Redox score ?

PDB code

2uxa

Structure name

crystal structure of the glur2-flip ligand binding domain, r/g unedited

Structure deposition date

2007-03-27

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Q9R174

Residue number A

739

Residue number B

794

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 739 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 794 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 739 and 773 (718 and 773 respectively in this structure).

Details

Redox score ?

PDB code

5fti

Structure name

crystal structure of the glua2 k738m-t744k lbd in complex with glutamate (lithium form)

Structure deposition date

2016-01-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

739

Residue number B

773

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 739 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 773 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 773 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 1219 and 330 (1219 and 1220 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7rza

Structure name

structure of the complex of ampa receptor glua2 with auxiliary subunit gsg1l bound to agonist quisqualate

Structure deposition date

2021-08-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

1219

Residue number B

330

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 1219 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 330 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1219 in protein A could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 104 and 330 (83 and 309 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer

Structure deposition date

2016-02-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide accession

Residue number A

104

Residue number B

330

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 104 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 330 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 739 and 258 (203 and 258 respectively in this structure).

Details

Redox score ?

nan

PDB code

2p2a

Structure name

x-ray structure of the glur2 ligand binding core (s1s2j) in complex with 2-bn-tet-ampa at 2

Structure deposition date

2007-03-07

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

739

Residue number B

258

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 739 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 258 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 258 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 739 and 261 (206 and 261 respectively in this structure).

Details

Redox score ?

nan

PDB code

2xhd

Structure name

crystal structure of n-((2s)-5-(6-fluoro-3-pyridinyl)-2,3- dihydro-1h-inden-2-yl)-2-propanesulfonamide in complex with the ligand binding domain of the human glua2 receptor

Structure deposition date

2010-06-14

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

P42262

Residue number A

739

Residue number B

261

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 739 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 261 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 261 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 739 and 1076 (1039 and 1076 respectively in this structure).

Details

Redox score ?

nan

PDB code

7tnn

Structure name

complex ggnn of ampa-subtype iglur glua2 in complex with auxiliary subunit gamma2 (stargazin) at low glutamate concentration (20 um) in the presence of cyclothiazide (100 um)

Structure deposition date

2022-01-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

739

Residue number B

1076

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 739 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1076 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1076 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 739 and 1066 (1039 and 1066 respectively in this structure).

Details

Redox score ?

nan

PDB code

7tnn

Structure name

complex ggnn of ampa-subtype iglur glua2 in complex with auxiliary subunit gamma2 (stargazin) at low glutamate concentration (20 um) in the presence of cyclothiazide (100 um)

Structure deposition date

2022-01-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

739

Residue number B

1066

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 739 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1066 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1066 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 739 and 1067 (1039 and 1067 respectively in this structure).

Details

Redox score ?

nan

PDB code

7tnn

Structure name

complex ggnn of ampa-subtype iglur glua2 in complex with auxiliary subunit gamma2 (stargazin) at low glutamate concentration (20 um) in the presence of cyclothiazide (100 um)

Structure deposition date

2022-01-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

739

Residue number B

1067

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 739 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1067 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1067 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 95 and 145.

Details

Redox score ?

nan

PDB code

3t9x

Structure name

glutamate bound to a double cysteine mutant (v484c/e657c) of the ligand binding domain of glua2

Structure deposition date

2011-08-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

Residue number B

145

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 95 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 145 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 95 in protein A could not be asigned to a Uniprot residue.

Cysteine 145 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 1099 and 1110.

Details

Redox score ?

nan

PDB code

7rz9

Structure name

structure of the complex of ampa receptor glua2 with auxiliary subunit gsg1l in the apo state

Structure deposition date

2021-08-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1099

Residue number B

1110

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 1099 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1110 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1099 in protein A could not be asigned to a Uniprot residue.

Cysteine 1110 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 73 and 134.

Details

Redox score ?

nan

PDB code

5n6p

Structure name

ampa receptor ntd mutant

Structure deposition date

2017-02-15

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

134

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 73 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 134 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 73 in protein A could not be asigned to a Uniprot residue.

Cysteine 134 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 63 and 794 (63 and 140 respectively in this structure).

Details

Redox score ?

nan

PDB code

3t9v

Structure name

cnqx bound to a reduced double cysteine mutant (a452c/s652c) of the ligand binding domain of glua2

Structure deposition date

2011-08-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

Residue number B

794

Peptide name

Glutamate receptor 2

Ligandability

Cysteine 63 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 794 of Glutamate receptor 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 63 in protein A could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Glutamate receptor 2 between cysteines 1067 and 1076.

Details

Redox score ?

nan

PDB code

7tno

Structure name

complex gggn of ampa-subtype iglur glua2 in complex with auxiliary subunit gamma2 (stargazin) at low glutamate concentration (20 um) in the presence of cyclothiazide (100 um)

Structure deposition date

2022-01-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession