Transducin-like enhancer protein 1
Intermolecular
Cysteine 89 and cysteine 89
Cysteine 47 and cysteine 47
Intramolecular
Cysteine 506 and cysteine 526
Cysteine 577 and cysteine 592
Cysteine 577 and cysteine 593
Cysteine 577 and cysteine 589
Cysteine 666 and cysteine 709
Cysteine 526 and cysteine 536
Cysteine 592 and cysteine 593
Cysteine 592 and cysteine 621
More...Cysteine 589 and cysteine 593
Cysteine 589 and cysteine 592
4om2 A 90 C 90
A redox-regulated disulphide may form between two units of Transducin-like enhancer protein 1 at cysteines 89 and 89 (90 and 90 respectively in this structure).
Details
Redox score ?
79
PDB code
4om2
Structure name
crystal structure of tle1 n-terminal q-domain residues 1-156
Structure deposition date
2014-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
57
Peptide A name
Transducin-like enhancer protein 1
Peptide B name
Transducin-like enhancer protein 1
Peptide A accession
Q04724
Peptide B accession
Q04724
Peptide A residue number
89
Peptide B residue number
89
Ligandability
4om2 B 48 D 48
A redox-regulated disulphide may form between two units of Transducin-like enhancer protein 1 at cysteines 47 and 47 (48 and 48 respectively in this structure).
Details
Redox score ?
79
PDB code
4om2
Structure name
crystal structure of tle1 n-terminal q-domain residues 1-156
Structure deposition date
2014-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
1
Peptide A name
Transducin-like enhancer protein 1
Peptide B name
Transducin-like enhancer protein 1
Peptide A accession
Q04724
Peptide B accession
Q04724
Peptide A residue number
47
Peptide B residue number
47
Ligandability
2ce9 D 506 D 526
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 506 and 526. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2ce9
Structure name
a wrpw peptide bound to the groucho-tle wd40 domain
Structure deposition date
2006-02-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
56
Peptide accession
Q04724
Residue number A
506
Residue number B
526
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 506 of Transducin-like enhancer protein 1
Cysteine 526 of Transducin-like enhancer protein 1
1gxr A 577 A 592
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 577 and 592. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
1gxr
Structure name
wd40 region of human groucho/tle1
Structure deposition date
2002-04-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
11
% buried
100
Peptide accession
Q04724
Residue number A
577
Residue number B
592
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 577 of Transducin-like enhancer protein 1
Cysteine 592 of Transducin-like enhancer protein 1
2ce8 C 577 C 593
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 577 and 593. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2ce8
Structure name
an eh1 peptide bound to the groucho-tle wd40 domain
Structure deposition date
2006-02-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
11
% buried
88
Peptide accession
Q04724
Residue number A
577
Residue number B
593
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 577 of Transducin-like enhancer protein 1
Cysteine 593 of Transducin-like enhancer protein 1
5mwj A 577 A 589
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 577 and 589. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5mwj
Structure name
structure enabled discovery of a stapled peptide inhibitor to target the oncogenic transcriptional repressor tle1
Structure deposition date
2017-01-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
100
Peptide accession
Q04724
Residue number A
577
Residue number B
589
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 577 of Transducin-like enhancer protein 1
Cysteine 589 of Transducin-like enhancer protein 1
2ce9 D 666 D 709
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 666 and 709. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2ce9
Structure name
a wrpw peptide bound to the groucho-tle wd40 domain
Structure deposition date
2006-02-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
54
Peptide accession
Q04724
Residue number A
666
Residue number B
709
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 666 of Transducin-like enhancer protein 1
Cysteine 709 of Transducin-like enhancer protein 1
2ce9 A 526 A 536
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 526 and 536. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2ce9
Structure name
a wrpw peptide bound to the groucho-tle wd40 domain
Structure deposition date
2006-02-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
92
Peptide accession
Q04724
Residue number A
526
Residue number B
536
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 526 of Transducin-like enhancer protein 1
Cysteine 536 of Transducin-like enhancer protein 1
5mwj B 592 B 593
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 592 and 593. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5mwj
Structure name
structure enabled discovery of a stapled peptide inhibitor to target the oncogenic transcriptional repressor tle1
Structure deposition date
2017-01-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
80
Peptide accession
Q04724
Residue number A
592
Residue number B
593
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 592 of Transducin-like enhancer protein 1
Cysteine 593 of Transducin-like enhancer protein 1
5mwj B 592 B 621
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 592 and 621. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5mwj
Structure name
structure enabled discovery of a stapled peptide inhibitor to target the oncogenic transcriptional repressor tle1
Structure deposition date
2017-01-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
100
Peptide accession
Q04724
Residue number A
592
Residue number B
621
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 592 of Transducin-like enhancer protein 1
Cysteine 621 of Transducin-like enhancer protein 1
2ce9 D 589 D 593
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 589 and 593. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
2ce9
Structure name
a wrpw peptide bound to the groucho-tle wd40 domain
Structure deposition date
2006-02-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
11
% buried
84
Peptide accession
Q04724
Residue number A
589
Residue number B
593
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 589 of Transducin-like enhancer protein 1
Cysteine 593 of Transducin-like enhancer protein 1
5mwj B 589 B 592
A redox-regulated disulphide may form within Transducin-like enhancer protein 1 between cysteines 589 and 592. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
5mwj
Structure name
structure enabled discovery of a stapled peptide inhibitor to target the oncogenic transcriptional repressor tle1
Structure deposition date
2017-01-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
94
Minimum pKa ?
13
% buried
96
Peptide accession
Q04724
Residue number A
589
Residue number B
592
Peptide name
Transducin-like enhancer protein 1
Ligandability
Cysteine 589 of Transducin-like enhancer protein 1
Cysteine 592 of Transducin-like enhancer protein 1
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