Trefoil factor 1
Intermolecular
Cysteine 82 and cysteine 82
Intramolecular
Cysteine 51 and cysteine 68
Cysteine 41 and cysteine 56
Cysteine 31 and cysteine 57
Cysteine 41 and cysteine 68
Cysteine 51 and cysteine 56
Cysteine 56 and cysteine 68
Cysteine 41 and cysteine 51
Cysteine 51 and cysteine 57
Cysteine 31 and cysteine 51
More...Cysteine 31 and cysteine 56
Cysteine 56 and cysteine 57
Cysteine 57 and cysteine 68
Cysteine 41 and cysteine 57
Cysteine 31 and cysteine 68
Cysteine 31 and cysteine 41
1hi7 A 58 B 58
A redox-regulated disulphide may form between two units of Trefoil factor 1 at cysteines 82 and 82 (58 and 58 respectively in this structure).
Details
Redox score ?
90
PDB code
1hi7
Structure name
nmr solution structure of the disulphide-linked homodimer of human tff1, 10 structures
Structure deposition date
2001-01-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
26
Minimum pKa ?
nan
% buried
nan
Peptide A name
Trefoil factor 1
Peptide B name
Trefoil factor 1
Peptide A accession
P04155
Peptide B accession
P04155
Peptide A residue number
82
Peptide B residue number
82
Ligandability
6v1d C 25 C 42
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 51 and 68 (25 and 42 respectively in this structure).
Details
Redox score ?
86
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
51
Residue number B
68
Peptide name
Trefoil factor 1
Ligandability
Cysteine 51 of Trefoil factor 1
Cysteine 68 of Trefoil factor 1
6v1d A 15 A 30
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 41 and 56 (15 and 30 respectively in this structure).
Details
Redox score ?
81
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
41
Residue number B
56
Peptide name
Trefoil factor 1
Ligandability
Cysteine 41 of Trefoil factor 1
Cysteine 56 of Trefoil factor 1
6v1d B 5 B 31
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 31 and 57 (5 and 31 respectively in this structure).
Details
Redox score ?
81
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
31
Residue number B
57
Peptide name
Trefoil factor 1
Ligandability
Cysteine 31 of Trefoil factor 1
Cysteine 57 of Trefoil factor 1
6v1d C 15 C 42
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 41 and 68 (15 and 42 respectively in this structure).
Details
Redox score ?
72
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
41
Residue number B
68
Peptide name
Trefoil factor 1
Ligandability
Cysteine 41 of Trefoil factor 1
Cysteine 68 of Trefoil factor 1
6v1d A 25 A 30
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 51 and 56 (25 and 30 respectively in this structure).
Details
Redox score ?
68
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
51
Residue number B
56
Peptide name
Trefoil factor 1
Ligandability
Cysteine 51 of Trefoil factor 1
Cysteine 56 of Trefoil factor 1
6v1d A 30 A 42
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 56 and 68 (30 and 42 respectively in this structure).
Details
Redox score ?
68
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
56
Residue number B
68
Peptide name
Trefoil factor 1
Ligandability
Cysteine 56 of Trefoil factor 1
Cysteine 68 of Trefoil factor 1
6v1d A 15 A 25
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 41 and 51 (15 and 25 respectively in this structure).
Details
Redox score ?
66
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
41
Residue number B
51
Peptide name
Trefoil factor 1
Ligandability
Cysteine 41 of Trefoil factor 1
Cysteine 51 of Trefoil factor 1
6v1d A 25 A 31
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 51 and 57 (25 and 31 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
51
Residue number B
57
Peptide name
Trefoil factor 1
Ligandability
Cysteine 51 of Trefoil factor 1
Cysteine 57 of Trefoil factor 1
6v1d C 5 C 25
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 31 and 51 (5 and 25 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
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
31
Residue number B
51
Peptide name
Trefoil factor 1
Ligandability
Cysteine 31 of Trefoil factor 1
Cysteine 51 of Trefoil factor 1
6v1d C 5 C 30
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 31 and 56 (5 and 30 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
31
Residue number B
56
Peptide name
Trefoil factor 1
Ligandability
Cysteine 31 of Trefoil factor 1
Cysteine 56 of Trefoil factor 1
6v1d B 30 B 31
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 56 and 57 (30 and 31 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
56
Residue number B
57
Peptide name
Trefoil factor 1
Ligandability
Cysteine 56 of Trefoil factor 1
Cysteine 57 of Trefoil factor 1
6v1d A 31 A 42
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 57 and 68 (31 and 42 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
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
57
Residue number B
68
Peptide name
Trefoil factor 1
Ligandability
Cysteine 57 of Trefoil factor 1
Cysteine 68 of Trefoil factor 1
6v1d C 15 C 31
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 41 and 57 (15 and 31 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
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
41
Residue number B
57
Peptide name
Trefoil factor 1
Ligandability
Cysteine 41 of Trefoil factor 1
Cysteine 57 of Trefoil factor 1
6v1d A 5 A 42
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 31 and 68 (5 and 42 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
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
31
Residue number B
68
Peptide name
Trefoil factor 1
Ligandability
Cysteine 31 of Trefoil factor 1
Cysteine 68 of Trefoil factor 1
6v1d C 5 C 15
A redox-regulated disulphide may form within Trefoil factor 1 between cysteines 31 and 41 (5 and 15 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
6v1d
Structure name
crystal structure of human trefoil factor 1
Structure deposition date
2019-11-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04155
Residue number A
31
Residue number B
41
Peptide name
Trefoil factor 1
Ligandability
Cysteine 31 of Trefoil factor 1
Cysteine 41 of Trefoil factor 1
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