ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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CASP8 and FADD-like apoptosis regulator

Intramolecular
Cysteine 298 and cysteine 345
Cysteine 254 and cysteine 310
Cysteine 259 and cysteine 310
A redox-regulated disulphide may form within CASP8 and FADD-like apoptosis regulator between cysteines 298 and 345. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3h13
Structure name
c-flipl protease-like domain
Structure deposition date
2009-04-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
28
Peptide accession
O15519
Residue number A
298
Residue number B
345
Peptide name
CASP8 and FADD-like apoptosis regulator

Ligandability

Cysteine 298 of CASP8 and FADD-like apoptosis regulator

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 345 of CASP8 and FADD-like apoptosis regulator

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 CASP8 and FADD-like apoptosis regulator between cysteines 254 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3h11
Structure name
zymogen caspase-8:c-flipl protease domain complex
Structure deposition date
2009-04-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
O15519
Residue number A
254
Residue number B
310
Peptide name
CASP8 and FADD-like apoptosis regulator

Ligandability

Cysteine 254 of CASP8 and FADD-like apoptosis regulator

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 310 of CASP8 and FADD-like apoptosis regulator

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 CASP8 and FADD-like apoptosis regulator between cysteines 259 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
3h11
Structure name
zymogen caspase-8:c-flipl protease domain complex
Structure deposition date
2009-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
85
Peptide accession
O15519
Residue number A
259
Residue number B
310
Peptide name
CASP8 and FADD-like apoptosis regulator

Ligandability

Cysteine 259 of CASP8 and FADD-like apoptosis regulator

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 310 of CASP8 and FADD-like apoptosis regulator

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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