Glutamate receptor 1

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

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 330 of Glutamate receptor 2 and cysteine 75 of Glutamate receptor 1 (309 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

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 ?

nan

% buried

nan

Peptide A name

Glutamate receptor 2

Peptide B name

Glutamate receptor 1

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 75 of Glutamate receptor 1

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 cysteine 75 of Glutamate receptor 1 and cysteine 78 of Glutamate receptor (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

7lde

Structure name

native ampa receptor

Structure deposition date

2021-01-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor

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

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 323 of Glutamate receptor 1 and cysteine 78 of Glutamate receptor (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

7ldd

Structure name

native ampa receptor

Structure deposition date

2021-01-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor

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

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 75 of Glutamate receptor 1 and cysteine 330 of Glutamate receptor (57 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

7ldd

Structure name

native ampa receptor

Structure deposition date

2021-01-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

330

Ligandability

Cysteine 75 of Glutamate receptor 1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 330 of Glutamate receptor

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 (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

7lde

Structure name

native ampa receptor

Structure deposition date

2021-01-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor

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

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 two units of Glutamate receptor 1 at cysteines 323 and 75 (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

3saj

Structure name

crystal structure of glutamate receptor glua1 amino terminal domain

Structure deposition date

2011-06-02

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor 1

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 75 of Glutamate receptor 1

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 two units of Glutamate receptor 1 at cysteines 603 and 603 (585 and 585 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

7qhb

Structure name

active state of glua1/2 in complex with tarp gamma 8, l-glutamate and ctz

Structure deposition date

2021-12-11

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor 1

Peptide A accession

Peptide B accession

Peptide A residue number

603

Peptide B residue number

603

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Glutamate receptor 1 at cysteines 75 and 75 (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

3saj

Structure name

crystal structure of glutamate receptor glua1 amino terminal domain

Structure deposition date

2011-06-02

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide A name

Glutamate receptor 1

Peptide B name

Glutamate receptor 1

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Glutamate receptor 1 between cysteines 732 and 787 (718 and 773 respectively in this structure).

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 accession

Residue number A

732

Residue number B

787

Peptide name

Glutamate receptor 1

Ligandability

Cysteine 732 of Glutamate receptor 1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 787 of Glutamate receptor 1

Not ligandable in the dataset of Vinogradova et al.