Cholinergic receptor nicotinic alpha 1 subunit

Intermolecular

Cysteine 212 and cysteine 54 of Alpha-bungarotoxin isoform V31

Intramolecular

A redox-regulated disulphide may form between cysteine 212 of Cholinergic receptor nicotinic alpha 1 subunit and cysteine 54 of Alpha-bungarotoxin isoform V31 (192 and 33 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

5hbt

Structure name

complex structure of fab35 and human nachr alpha1

Structure deposition date

2016-01-02

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Cholinergic receptor nicotinic alpha 1 subunit

Peptide B name

Alpha-bungarotoxin isoform V31

Peptide A accession

G5E9G9

Peptide B accession

P60616

Peptide A residue number

212

Peptide B residue number

Ligandability

Cysteine 212 of Cholinergic receptor nicotinic alpha 1 subunit

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 54 of Alpha-bungarotoxin isoform V31

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 Cholinergic receptor nicotinic alpha 1 subunit between cysteines 148 and 162 (128 and 142 respectively in this structure).

Details

Redox score ?

PDB code

5hbt

Structure name

complex structure of fab35 and human nachr alpha1

Structure deposition date

2016-01-02

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

G5E9G9

Residue number A

148

Residue number B

162

Peptide name

Cholinergic receptor nicotinic alpha 1 subunit

Ligandability

Cysteine 148 of Cholinergic receptor nicotinic alpha 1 subunit

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 162 of Cholinergic receptor nicotinic alpha 1 subunit

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 Cholinergic receptor nicotinic alpha 1 subunit between cysteines 212 and 213 (192 and 193 respectively in this structure).