Spermine synthase

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Spermine synthase at cysteines 347 and 347 (349 and 349 respectively in this structure).

Details

Redox score ?

PDB code

3c6k

Structure name

crystal structure of human spermine synthase in complex with spermidine and 5-methylthioadenosine

Structure deposition date

2008-02-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Spermine synthase

Peptide B name

Spermine synthase

Peptide A accession

P52788

Peptide B accession

P52788

Peptide A residue number

347

Peptide B residue number

347

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 Spermine synthase between cysteines 229 and 237. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3c6m

Structure name

crystal structure of human spermine synthase in complex with spermine and 5-methylthioadenosine

Structure deposition date

2008-02-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P52788

Residue number A

229

Residue number B

237

Peptide name

Spermine synthase

Ligandability

Cysteine 229 of Spermine synthase

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 237 of Spermine synthase

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 Spermine synthase between cysteines 206 and 237. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?