Immunoglobulin heavy constant gamma 1

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Immunoglobulin heavy constant gamma 1 at cysteines 336 and 336 (457 and 457 respectively in this structure).

Details

Redox score ?

PDB code

7wso

Structure name

structure of a membrane protein g

Structure deposition date

2022-01-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Immunoglobulin heavy constant gamma 1

Peptide B name

Immunoglobulin heavy constant gamma 1

Peptide A accession

A0A0A0MS08

Peptide B accession

A0A0A0MS08

Peptide A residue number

336

Peptide B residue number

336

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Immunoglobulin heavy constant gamma 1 between cysteines 250 and 308 (371 and 429 respectively in this structure).

Details

Redox score ?

PDB code

7wso

Structure name

structure of a membrane protein g

Structure deposition date

2022-01-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

A0A0A0MS08

Residue number A

250

Residue number B

308

Peptide name

Immunoglobulin heavy constant gamma 1

Ligandability

Cysteine 250 of Immunoglobulin heavy constant gamma 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 308 of Immunoglobulin heavy constant gamma 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Immunoglobulin heavy constant gamma 1 between cysteines 144 and 204 (265 and 325 respectively in this structure).