ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

NF-kappa-B essential modulator

Intermolecular
Cysteine 54 and cysteine 54
Cysteine 716 of Inhibitor of nuclear factor kappa-B kinase subunit beta and cysteine 76
Cysteine 114 of Inhibitor of nuclear factor kappa-B kinase subunit alpha and cysteine 76
Intramolecular
Cysteine 397 and cysteine 417
Cysteine 397 and cysteine 400
Cysteine 400 and cysteine 417
Cysteine 396 and cysteine 397
Cysteine 396 and cysteine 400
Cysteine 396 and cysteine 417
A redox-regulated disulphide may form between two units of NF-kappa-B essential modulator at cysteines 54 and 54.

Details

Redox score ?
84
PDB code
3brv
Structure name
nemo/ikkb association domain structure
Structure deposition date
2007-12-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
1
Peptide A name
NF-kappa-B essential modulator
Peptide B name
NF-kappa-B essential modulator
Peptide A accession
Q9Y6K9
Peptide B accession
Q9Y6K9
Peptide A residue number
54
Peptide B residue number
54

Ligandability

A redox-regulated disulphide may form between cysteine 716 of Inhibitor of nuclear factor kappa-B kinase subunit beta and cysteine 76 of NF-kappa-B essential modulator. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3brv
Structure name
nemo/ikkb association domain structure
Structure deposition date
2007-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
54
Peptide A name
Inhibitor of nuclear factor kappa-B kinase subunit beta
Peptide B name
NF-kappa-B essential modulator
Peptide A accession
O14920
Peptide B accession
Q9Y6K9
Peptide A residue number
716
Peptide B residue number
76

Ligandability

Cysteine 716 of Inhibitor of nuclear factor kappa-B kinase subunit beta

Cysteine 76 of NF-kappa-B essential modulator

A redox-regulated disulphide may form between cysteine 114 of Inhibitor of nuclear factor kappa-B kinase subunit alpha and cysteine 76 of NF-kappa-B essential modulator (716 and 76 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3brt
Structure name
nemo/ikk association domain structure
Structure deposition date
2007-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
58
Peptide A name
Inhibitor of nuclear factor kappa-B kinase subunit alpha
Peptide B name
NF-kappa-B essential modulator
Peptide A accession
O15111
Peptide B accession
Q9Y6K9
Peptide A residue number
114
Peptide B residue number
76

Ligandability

Cysteine 114 of Inhibitor of nuclear factor kappa-B kinase subunit alpha

Cysteine 76 of NF-kappa-B essential modulator

A redox-regulated disulphide may form within NF-kappa-B essential modulator between cysteines 397 and 417 (6 and 26 respectively in this structure).

Details

Redox score ?
89
PDB code
2jvx
Structure name
solution structure of human nemo zinc finger
Structure deposition date
2007-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
7
% buried
0
Peptide accession
Q9Y6K9
Residue number A
397
Residue number B
417
Peptide name
NF-kappa-B essential modulator

Ligandability

Cysteine 397 of NF-kappa-B essential modulator

Cysteine 417 of NF-kappa-B essential modulator

A redox-regulated disulphide may form within NF-kappa-B essential modulator between cysteines 397 and 400 (6 and 9 respectively in this structure).

Details

Redox score ?
87
PDB code
2jvx
Structure name
solution structure of human nemo zinc finger
Structure deposition date
2007-09-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
7
% buried
0
Peptide accession
Q9Y6K9
Residue number A
397
Residue number B
400
Peptide name
NF-kappa-B essential modulator

Ligandability

Cysteine 397 of NF-kappa-B essential modulator

Cysteine 400 of NF-kappa-B essential modulator

A redox-regulated disulphide may form within NF-kappa-B essential modulator between cysteines 400 and 417.

Details

Redox score ?
84
PDB code
5aay
Structure name
tbk1 recruitment to cytosol-invading salmonella induces anti- bacterial autophagy
Structure deposition date
2015-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
31
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y6K9
Residue number A
400
Residue number B
417
Peptide name
NF-kappa-B essential modulator

Ligandability

Cysteine 400 of NF-kappa-B essential modulator

Cysteine 417 of NF-kappa-B essential modulator

A redox-regulated disulphide may form within NF-kappa-B essential modulator between cysteines 396 and 397 (5 and 6 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2jvy
Structure name
solution structure of the eda-id-related c417f mutant of human nemo zinc finger
Structure deposition date
2007-09-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
Q9Y6K9
Residue number A
396
Residue number B
397
Peptide name
NF-kappa-B essential modulator

Ligandability

Cysteine 396 of NF-kappa-B essential modulator

Cysteine 397 of NF-kappa-B essential modulator

A redox-regulated disulphide may form within NF-kappa-B essential modulator between cysteines 396 and 400 (5 and 9 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2jvy
Structure name
solution structure of the eda-id-related c417f mutant of human nemo zinc finger
Structure deposition date
2007-09-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
33
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y6K9
Residue number A
396
Residue number B
400
Peptide name
NF-kappa-B essential modulator

Ligandability

Cysteine 396 of NF-kappa-B essential modulator

Cysteine 400 of NF-kappa-B essential modulator

A redox-regulated disulphide may form within NF-kappa-B essential modulator between cysteines 396 and 417 (5 and 26 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2jvx
Structure name
solution structure of human nemo zinc finger
Structure deposition date
2007-09-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
37
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y6K9
Residue number A
396
Residue number B
417
Peptide name
NF-kappa-B essential modulator

Ligandability

Cysteine 396 of NF-kappa-B essential modulator

Cysteine 417 of NF-kappa-B essential modulator

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