ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prothrombin

Intermolecular
Cysteine 333 and cysteine 479
Intramolecular
Cysteine 561 and cysteine 591
Cysteine 533 and cysteine 547
Cysteine 388 and cysteine 404 L
A redox-regulated disulphide may form between two units of Prothrombin at cysteines 333 and 479 (1 and 122 respectively in this structure).

Details

Redox score ?
80
PDB code
2ocv
Structure name
structural basis of na+ activation mimicry in murine thrombin
Structure deposition date
2006-12-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prothrombin
Peptide B name
Prothrombin
Peptide A accession
P19221
Peptide B accession
P19221
Peptide A residue number
333
Peptide B residue number
479

Ligandability

Cysteine 333 of Prothrombin

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 479 of Prothrombin

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 Prothrombin between cysteines 561 and 591 (191 and 220 respectively in this structure).

Details

Redox score ?
85
PDB code
3hki
Structure name
crystal structure of murine thrombin mutant w215a/e217a in complex with the extracellular fragment of human par1
Structure deposition date
2009-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19221
Residue number A
561
Residue number B
591
Peptide name
Prothrombin

Ligandability

Cysteine 561 of Prothrombin

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 591 of Prothrombin

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 Prothrombin between cysteines 533 and 547 (168 and 182 respectively in this structure).

Details

Redox score ?
81
PDB code
2pv9
Structure name
crystal structure of murine thrombin in complex with the extracellular fragment of murine par4
Structure deposition date
2007-05-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19221
Residue number A
533
Residue number B
547
Peptide name
Prothrombin

Ligandability

Cysteine 533 of Prothrombin

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 547 of Prothrombin

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 Prothrombin between cysteines 388 and 404 (42 and 58 respectively in this structure).

Details

Redox score ?
79
PDB code
2ocv
Structure name
structural basis of na+ activation mimicry in murine thrombin
Structure deposition date
2006-12-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19221
Residue number A
388
Residue number B
404
Peptide name
Prothrombin

Ligandability

Cysteine 388 of Prothrombin

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.

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 404 of Prothrombin

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.

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