Gamma-crystallin C
Intramolecular
Cysteine 19 and cysteine 23
Cysteine 23 and cysteine 79
Cysteine 109 and cysteine 111
Cysteine 79 and cysteine 80
Cysteine 23 and cysteine 80
Cysteine 42 and cysteine 130
Cysteine 33 and cysteine 79
Cysteine 80 and cysteine 130
2v2u B 18 B 22
A redox-regulated disulphide may form within Gamma-crystallin C between cysteines 19 and 23 (18 and 22 respectively in this structure).
Details
Redox score ?
74
PDB code
2v2u
Structure name
structure of mouse gammac-crystallin
Structure deposition date
2007-06-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
44
Peptide accession
Q61597
Residue number A
19
Residue number B
23
Peptide name
Gamma-crystallin C
Ligandability
Cysteine 19 of Gamma-crystallin C
Cysteine 23 of Gamma-crystallin C
2nbr A 22 A 78
A redox-regulated disulphide may form within Gamma-crystallin C between cysteines 23 and 79 (22 and 78 respectively in this structure).
Details
Redox score ?
66
PDB code
2nbr
Structure name
the solution structure of human gammac-crystallin
Structure deposition date
2016-03-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
48
Peptide accession
P07315
Residue number A
23
Residue number B
79
Peptide name
Gamma-crystallin C
Ligandability
Cysteine 23 of Gamma-crystallin C
Cysteine 79 of Gamma-crystallin C
2v2u B 108 B 110
A redox-regulated disulphide may form within Gamma-crystallin C between cysteines 109 and 111 (108 and 110 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2v2u
Structure name
structure of mouse gammac-crystallin
Structure deposition date
2007-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
18
Peptide accession
Q61597
Residue number A
109
Residue number B
111
Peptide name
Gamma-crystallin C
Ligandability
Cysteine 109 of Gamma-crystallin C
Cysteine 111 of Gamma-crystallin C
2nbr A 78 A 79
A redox-regulated disulphide may form within Gamma-crystallin C between cysteines 79 and 80 (78 and 79 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
2nbr
Structure name
the solution structure of human gammac-crystallin
Structure deposition date
2016-03-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
73
Peptide accession
P07315
Residue number A
79
Residue number B
80
Peptide name
Gamma-crystallin C
Ligandability
Cysteine 79 of Gamma-crystallin C
Cysteine 80 of Gamma-crystallin C
2nbr A 22 A 79
A redox-regulated disulphide may form within Gamma-crystallin C between cysteines 23 and 80 (22 and 79 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
2nbr
Structure name
the solution structure of human gammac-crystallin
Structure deposition date
2016-03-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
46
Peptide accession
P07315
Residue number A
23
Residue number B
80
Peptide name
Gamma-crystallin C
Ligandability
Cysteine 23 of Gamma-crystallin C
Cysteine 80 of Gamma-crystallin C
2nbr A 41 A 129
A redox-regulated disulphide may form within Gamma-crystallin C between cysteines 42 and 130 (41 and 129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
2nbr
Structure name
the solution structure of human gammac-crystallin
Structure deposition date
2016-03-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
63
Peptide accession
P07315
Residue number A
42
Residue number B
130
Peptide name
Gamma-crystallin C
Ligandability
Cysteine 42 of Gamma-crystallin C
Cysteine 130 of Gamma-crystallin C
2nbr A 32 A 78
A redox-regulated disulphide may form within Gamma-crystallin C between cysteines 33 and 79 (32 and 78 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
2nbr
Structure name
the solution structure of human gammac-crystallin
Structure deposition date
2016-03-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
87
Peptide accession
P07315
Residue number A
33
Residue number B
79
Peptide name
Gamma-crystallin C
Ligandability
Cysteine 33 of Gamma-crystallin C
Cysteine 79 of Gamma-crystallin C
2nbr A 79 A 129
A redox-regulated disulphide may form within Gamma-crystallin C between cysteines 80 and 130 (79 and 129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
2nbr
Structure name
the solution structure of human gammac-crystallin
Structure deposition date
2016-03-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
66
Peptide accession
P07315
Residue number A
80
Residue number B
130
Peptide name
Gamma-crystallin C
Ligandability
Cysteine 80 of Gamma-crystallin C
Cysteine 130 of Gamma-crystallin C
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