ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Acyl-CoA dehydrogenase family member 11

Intramolecular
Cysteine 503 and cysteine 547
Cysteine 503 and cysteine 505
Cysteine 505 and cysteine 547
Cysteine 505 and cysteine 521
A redox-regulated disulphide may form within Acyl-CoA dehydrogenase family member 11 between cysteines 503 and 547 (151 and 195 respectively in this structure).

Details

Redox score ?
70
PDB code
2wbi
Structure name
crystal structure of human acyl-coa dehydrogenase 11
Structure deposition date
2009-02-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q709F0
Residue number A
503
Residue number B
547
Peptide name
Acyl-CoA dehydrogenase family member 11

Ligandability

Cysteine 503 of Acyl-CoA dehydrogenase family member 11

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 Acyl-CoA dehydrogenase family member 11

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 Acyl-CoA dehydrogenase family member 11 between cysteines 503 and 505 (151 and 153 respectively in this structure).

Details

Redox score ?
68
PDB code
2wbi
Structure name
crystal structure of human acyl-coa dehydrogenase 11
Structure deposition date
2009-02-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q709F0
Residue number A
503
Residue number B
505
Peptide name
Acyl-CoA dehydrogenase family member 11

Ligandability

Cysteine 503 of Acyl-CoA dehydrogenase family member 11

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 505 of Acyl-CoA dehydrogenase family member 11

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 Acyl-CoA dehydrogenase family member 11 between cysteines 505 and 547 (153 and 195 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2wbi
Structure name
crystal structure of human acyl-coa dehydrogenase 11
Structure deposition date
2009-02-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q709F0
Residue number A
505
Residue number B
547
Peptide name
Acyl-CoA dehydrogenase family member 11

Ligandability

Cysteine 505 of Acyl-CoA dehydrogenase family member 11

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 Acyl-CoA dehydrogenase family member 11

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 Acyl-CoA dehydrogenase family member 11 between cysteines 505 and 521 (153 and 169 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
2wbi
Structure name
crystal structure of human acyl-coa dehydrogenase 11
Structure deposition date
2009-02-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q709F0
Residue number A
505
Residue number B
521
Peptide name
Acyl-CoA dehydrogenase family member 11

Ligandability

Cysteine 505 of Acyl-CoA dehydrogenase family member 11

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 521 of Acyl-CoA dehydrogenase family member 11

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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