ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Platelet glycoprotein Ib alpha chain

Intramolecular
Cysteine 227 and cysteine 280
Cysteine 20 and cysteine 33
Cysteine 225 and cysteine 264
Cysteine 225 and cysteine 280
Cysteine 225 and cysteine 227
Cysteine 33 and cysteine 81
A redox-regulated disulphide may form within Platelet glycoprotein Ib alpha chain between cysteines 227 and 280 (211 and 264 respectively in this structure).

Details

Redox score ?
87
PDB code
1ook
Structure name
crystal structure of the complex of platelet receptor gpib-alpha and human alpha-thrombin
Structure deposition date
2003-03-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07359
Residue number A
227
Residue number B
280
Peptide name
Platelet glycoprotein Ib alpha chain

Ligandability

Cysteine 227 of Platelet glycoprotein Ib alpha 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 280 of Platelet glycoprotein Ib alpha 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 Platelet glycoprotein Ib alpha chain between cysteines 20 and 33 (4 and 17 respectively in this structure).

Details

Redox score ?
85
PDB code
4c2a
Structure name
crystal structure of high-affinity von willebrand factor a1 domain with r1306q and i1309v mutations in complex with high affinity gpib alpha
Structure deposition date
2013-08-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07359
Residue number A
20
Residue number B
33
Peptide name
Platelet glycoprotein Ib alpha chain

Ligandability

Cysteine 20 of Platelet glycoprotein Ib alpha 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 33 of Platelet glycoprotein Ib alpha 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 Platelet glycoprotein Ib alpha chain between cysteines 225 and 264 (209 and 248 respectively in this structure).

Details

Redox score ?
84
PDB code
1u0n
Structure name
the ternary von willebrand factor a1-glycoprotein ibalpha-botrocetin complex
Structure deposition date
2004-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07359
Residue number A
225
Residue number B
264
Peptide name
Platelet glycoprotein Ib alpha chain

Ligandability

Cysteine 225 of Platelet glycoprotein Ib alpha 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 264 of Platelet glycoprotein Ib alpha 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 Platelet glycoprotein Ib alpha chain between cysteines 225 and 280 (209 and 264 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1qyy
Structure name
crystal structure of n-terminal domain of human platelet receptor glycoprotein ib-alpha at 2
Structure deposition date
2003-09-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07359
Residue number A
225
Residue number B
280
Peptide name
Platelet glycoprotein Ib alpha chain

Ligandability

Cysteine 225 of Platelet glycoprotein Ib alpha 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 280 of Platelet glycoprotein Ib alpha 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 Platelet glycoprotein Ib alpha chain between cysteines 225 and 227. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1gwb
Structure name
structure of glycoprotein 1b
Structure deposition date
2002-03-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07359
Residue number A
225
Residue number B
227
Peptide name
Platelet glycoprotein Ib alpha chain

Ligandability

Cysteine 225 of Platelet glycoprotein Ib alpha 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 227 of Platelet glycoprotein Ib alpha 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 Platelet glycoprotein Ib alpha chain between cysteines 33 and 81 (19 and 67 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6ejx
Structure name
the metal ion-dependent adhesion site (midas) of the alphambeta2 integrin mac-1 i-domain promiscuously and competitively binds multiple ligands in the regulation of leukocyte function
Structure deposition date
2017-09-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
nan
Peptide accession
O35930
Residue number A
33
Residue number B
81
Peptide name
Platelet glycoprotein Ib alpha chain

Ligandability

Cysteine 33 of Platelet glycoprotein Ib alpha 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 81 of Platelet glycoprotein Ib alpha 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.

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