ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Agouti-related protein

Intramolecular
Cysteine 101 and cysteine 119
Cysteine 87 and cysteine 102
Cysteine 110 and cysteine 117
Cysteine 94 and cysteine 108
Cysteine 105 and cysteine 129
Cysteine 108 and cysteine 117
Cysteine 94 and cysteine 119
Cysteine 101 and cysteine 108
Cysteine 94 and cysteine 117
Cysteine 108 and cysteine 110
More...
Cysteine 108 and cysteine 119
Cysteine 94 and cysteine 110
Cysteine 87 and cysteine 101
Cysteine 101 and cysteine 102
Cysteine 117 and cysteine 119
Cysteine 94 and cysteine 101
Cysteine 87 and cysteine 119
Cysteine 101 and cysteine 117
Cysteine 101 and cysteine 110
Cysteine 110 and cysteine 119
Cysteine 101 and cysteine 105
Cysteine 102 and cysteine 119
Cysteine 105 and cysteine 119
A redox-regulated disulphide may form within Agouti-related protein between cysteines 101 and 119 (15 and 33 respectively in this structure).

Details

Redox score ?
89
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
101
Residue number B
119
Peptide name
Agouti-related protein

Ligandability

Cysteine 101 of Agouti-related protein

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 119 of Agouti-related protein

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 Agouti-related protein between cysteines 87 and 102 (1 and 16 respectively in this structure).

Details

Redox score ?
89
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
87
Residue number B
102
Peptide name
Agouti-related protein

Ligandability

Cysteine 87 of Agouti-related protein

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 102 of Agouti-related protein

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 Agouti-related protein between cysteines 110 and 117 (24 and 31 respectively in this structure).

Details

Redox score ?
87
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
110
Residue number B
117
Peptide name
Agouti-related protein

Ligandability

Cysteine 110 of Agouti-related protein

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 117 of Agouti-related protein

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 Agouti-related protein between cysteines 94 and 108 (8 and 22 respectively in this structure).

Details

Redox score ?
87
PDB code
1hyk
Structure name
agouti-related protein (87-132) (ac-agrp(87-132))
Structure deposition date
2001-01-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
94
Residue number B
108
Peptide name
Agouti-related protein

Ligandability

Cysteine 94 of Agouti-related protein

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 108 of Agouti-related protein

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 Agouti-related protein between cysteines 105 and 129 (19 and 43 respectively in this structure).

Details

Redox score ?
85
PDB code
1hyk
Structure name
agouti-related protein (87-132) (ac-agrp(87-132))
Structure deposition date
2001-01-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
105
Residue number B
129
Peptide name
Agouti-related protein

Ligandability

Cysteine 105 of Agouti-related protein

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 129 of Agouti-related protein

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 Agouti-related protein between cysteines 108 and 117 (22 and 31 respectively in this structure).

Details

Redox score ?
74
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
108
Residue number B
117
Peptide name
Agouti-related protein

Ligandability

Cysteine 108 of Agouti-related protein

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 117 of Agouti-related protein

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 Agouti-related protein between cysteines 94 and 119 (8 and 33 respectively in this structure).

Details

Redox score ?
71
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
94
Residue number B
119
Peptide name
Agouti-related protein

Ligandability

Cysteine 94 of Agouti-related protein

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 119 of Agouti-related protein

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 Agouti-related protein between cysteines 101 and 108 (15 and 22 respectively in this structure).

Details

Redox score ?
68
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
101
Residue number B
108
Peptide name
Agouti-related protein

Ligandability

Cysteine 101 of Agouti-related protein

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 108 of Agouti-related protein

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 Agouti-related protein between cysteines 94 and 117 (8 and 31 respectively in this structure).

Details

Redox score ?
67
PDB code
1hyk
Structure name
agouti-related protein (87-132) (ac-agrp(87-132))
Structure deposition date
2001-01-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
94
Residue number B
117
Peptide name
Agouti-related protein

Ligandability

Cysteine 94 of Agouti-related protein

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 117 of Agouti-related protein

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 Agouti-related protein between cysteines 108 and 110 (22 and 24 respectively in this structure).

Details

Redox score ?
65
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
108
Residue number B
110
Peptide name
Agouti-related protein

Ligandability

Cysteine 108 of Agouti-related protein

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 110 of Agouti-related protein

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 Agouti-related protein between cysteines 108 and 119 (22 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
1hyk
Structure name
agouti-related protein (87-132) (ac-agrp(87-132))
Structure deposition date
2001-01-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
108
Residue number B
119
Peptide name
Agouti-related protein

Ligandability

Cysteine 108 of Agouti-related protein

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 119 of Agouti-related protein

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 Agouti-related protein between cysteines 94 and 110 (8 and 24 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
94
Residue number B
110
Peptide name
Agouti-related protein

Ligandability

Cysteine 94 of Agouti-related protein

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 110 of Agouti-related protein

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 Agouti-related protein between cysteines 87 and 101 (1 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 ?
57
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
87
Residue number B
101
Peptide name
Agouti-related protein

Ligandability

Cysteine 87 of Agouti-related protein

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 101 of Agouti-related protein

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 Agouti-related protein between cysteines 101 and 102 (15 and 16 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
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
101
Residue number B
102
Peptide name
Agouti-related protein

Ligandability

Cysteine 101 of Agouti-related protein

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 102 of Agouti-related protein

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 Agouti-related protein between cysteines 117 and 119 (31 and 33 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
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
117
Residue number B
119
Peptide name
Agouti-related protein

Ligandability

Cysteine 117 of Agouti-related protein

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 119 of Agouti-related protein

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 Agouti-related protein between cysteines 94 and 101 (8 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 ?
49
PDB code
1hyk
Structure name
agouti-related protein (87-132) (ac-agrp(87-132))
Structure deposition date
2001-01-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
94
Residue number B
101
Peptide name
Agouti-related protein

Ligandability

Cysteine 94 of Agouti-related protein

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 101 of Agouti-related protein

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 Agouti-related protein between cysteines 87 and 119 (1 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1hyk
Structure name
agouti-related protein (87-132) (ac-agrp(87-132))
Structure deposition date
2001-01-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
87
Residue number B
119
Peptide name
Agouti-related protein

Ligandability

Cysteine 87 of Agouti-related protein

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 119 of Agouti-related protein

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 Agouti-related protein between cysteines 101 and 117 (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 ?
45
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
101
Residue number B
117
Peptide name
Agouti-related protein

Ligandability

Cysteine 101 of Agouti-related protein

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 117 of Agouti-related protein

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 Agouti-related protein between cysteines 101 and 110 (15 and 24 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
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
101
Residue number B
110
Peptide name
Agouti-related protein

Ligandability

Cysteine 101 of Agouti-related protein

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 110 of Agouti-related protein

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 Agouti-related protein between cysteines 110 and 119 (24 and 33 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
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
110
Residue number B
119
Peptide name
Agouti-related protein

Ligandability

Cysteine 110 of Agouti-related protein

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 119 of Agouti-related protein

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 Agouti-related protein between cysteines 101 and 105 (15 and 19 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1hyk
Structure name
agouti-related protein (87-132) (ac-agrp(87-132))
Structure deposition date
2001-01-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
101
Residue number B
105
Peptide name
Agouti-related protein

Ligandability

Cysteine 101 of Agouti-related protein

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 105 of Agouti-related protein

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 Agouti-related protein between cysteines 102 and 119 (16 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1mr0
Structure name
solution nmr structure of agrp(87-120; c105a)
Structure deposition date
2002-09-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
102
Residue number B
119
Peptide name
Agouti-related protein

Ligandability

Cysteine 102 of Agouti-related protein

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 119 of Agouti-related protein

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 Agouti-related protein between cysteines 105 and 119 (19 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1hyk
Structure name
agouti-related protein (87-132) (ac-agrp(87-132))
Structure deposition date
2001-01-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
O00253
Residue number A
105
Residue number B
119
Peptide name
Agouti-related protein

Ligandability

Cysteine 105 of Agouti-related protein

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 119 of Agouti-related protein

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.

If this tool was useful for finding a disulphide, please cite: