Coagulation factor XIII A chain

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Coagulation factor XIII A chain at cysteines 424 and 424 (423 and 423 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

1ggu

Structure name

human factor xiii with calcium bound in the ion site

Structure deposition date

1998-07-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Coagulation factor XIII A chain

Peptide B name

Coagulation factor XIII A chain

Peptide A accession

P00488

Peptide B accession

P00488

Peptide A residue number

424

Peptide B residue number

424

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 Coagulation factor XIII A chain between cysteines 239 and 328 (238 and 327 respectively in this structure).

Details

Redox score ?

PDB code

1ggy

Structure name

human factor xiii with ytterbium bound in the ion site

Structure deposition date

1998-07-23

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

P00488

Residue number A

239

Residue number B

328

Peptide name

Coagulation factor XIII A chain

Ligandability

Cysteine 239 of Coagulation factor XIII A chain

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 328 of Coagulation factor XIII A chain

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 Coagulation factor XIII A chain between cysteines 315 and 375 (314 and 374 respectively in this structure).