ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Antigen peptide transporter 1

Intermolecular
Cysteine 442 of Coagulation factor X and cysteine 5
Cysteine 442 of Coagulation factor X and cysteine 59
Cysteine 414 of Coagulation factor X and cysteine 5
Intramolecular
Cysteine 698 and cysteine 712
A redox-regulated disulphide may form between cysteine 442 of Coagulation factor X and cysteine 5 of Tick anticoagulant peptide (220 and 505 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1kig
Structure name
bovine factor xa
Structure deposition date
1997-04-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Tick anticoagulant peptide
Peptide A accession
P00743
Peptide B accession
P17726
Peptide A residue number
442
Peptide B residue number
5

Ligandability

Cysteine 442 of Coagulation factor X

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 5 of Tick anticoagulant peptide

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 between cysteine 442 of Coagulation factor X and cysteine 59 of Tick anticoagulant peptide (220 and 559 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1kig
Structure name
bovine factor xa
Structure deposition date
1997-04-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Tick anticoagulant peptide
Peptide A accession
P00743
Peptide B accession
P17726
Peptide A residue number
442
Peptide B residue number
59

Ligandability

Cysteine 442 of Coagulation factor X

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 59 of Tick anticoagulant peptide

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 between cysteine 414 of Coagulation factor X and cysteine 5 of Tick anticoagulant peptide (191 and 505 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
1kig
Structure name
bovine factor xa
Structure deposition date
1997-04-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Tick anticoagulant peptide
Peptide A accession
P00743
Peptide B accession
P17726
Peptide A residue number
414
Peptide B residue number
5

Ligandability

Cysteine 414 of Coagulation factor X

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 5 of Tick anticoagulant peptide

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 Antigen peptide transporter 1 between cysteines 698 and 712.

Details

Redox score ?
79
PDB code
2ixe
Structure name
crystal structure of the atpase domain of tap1 with atp (d645n mutant)
Structure deposition date
2006-07-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
14
Peptide accession
P36370
Residue number A
698
Residue number B
712
Peptide name
Antigen peptide transporter 1

Ligandability

Cysteine 698 of Antigen peptide transporter 1

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 712 of Antigen peptide transporter 1

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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