Elafin
Intermolecular
Cysteine 109 and cysteine 109
Cysteine 72 of Chymotrypsin-like elastase family member 1 and cysteine 109
Cysteine 72 of Chymotrypsin-like elastase family member 1 and cysteine 83
Cysteine 56 of Chymotrypsin-like elastase family member 1 and cysteine 109
Cysteine 56 of Chymotrypsin-like elastase family member 1 and cysteine 83
Cysteine 83 and cysteine 109
Cysteine 83 and cysteine 83
Intramolecular
Cysteine 98 and cysteine 113
Cysteine 76 and cysteine 105
Cysteine 92 and cysteine 104
More...Cysteine 92 and cysteine 98
Cysteine 92 and cysteine 113
Cysteine 98 and cysteine 104
Cysteine 104 and cysteine 113
Cysteine 98 and cysteine 105
Cysteine 104 and cysteine 105
Cysteine 92 and cysteine 105
Cysteine 76 and cysteine 104
Cysteine 76 and cysteine 98
Cysteine 76 and cysteine 92
Cysteine 105 and cysteine 113
Cysteine 76 and cysteine 113
6atu B 49 E 49
A redox-regulated disulphide may form between two units of Elafin at cysteines 109 and 109 (49 and 49 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide A name
Elafin
Peptide B name
Elafin
Peptide A accession
P19957
Peptide B accession
P19957
Peptide A residue number
109
Peptide B residue number
109
Ligandability
1fle E 58 I 49
A redox-regulated disulphide may form between cysteine 72 of Chymotrypsin-like elastase family member 1 and cysteine 109 of Elafin (58 and 49 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
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Elafin
Peptide A accession
P00772
Peptide B accession
P19957
Peptide A residue number
72
Peptide B residue number
109
Ligandability
Cysteine 72 of Chymotrypsin-like elastase family member 1
Cysteine 109 of Elafin
1fle E 58 I 23
A redox-regulated disulphide may form between cysteine 72 of Chymotrypsin-like elastase family member 1 and cysteine 83 of Elafin (58 and 23 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
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Elafin
Peptide A accession
P00772
Peptide B accession
P19957
Peptide A residue number
72
Peptide B residue number
83
Ligandability
Cysteine 72 of Chymotrypsin-like elastase family member 1
Cysteine 83 of Elafin
1fle E 42 I 49
A redox-regulated disulphide may form between cysteine 56 of Chymotrypsin-like elastase family member 1 and cysteine 109 of Elafin (42 and 49 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
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Elafin
Peptide A accession
P00772
Peptide B accession
P19957
Peptide A residue number
56
Peptide B residue number
109
Ligandability
Cysteine 56 of Chymotrypsin-like elastase family member 1
Cysteine 109 of Elafin
1fle E 42 I 23
A redox-regulated disulphide may form between cysteine 56 of Chymotrypsin-like elastase family member 1 and cysteine 83 of Elafin (42 and 23 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
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Elafin
Peptide A accession
P00772
Peptide B accession
P19957
Peptide A residue number
56
Peptide B residue number
83
Ligandability
Cysteine 56 of Chymotrypsin-like elastase family member 1
Cysteine 83 of Elafin
6atu A 23 I 49
A redox-regulated disulphide may form between two units of Elafin at cysteines 83 and 109 (23 and 49 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Elafin
Peptide B name
Elafin
Peptide A accession
P19957
Peptide B accession
P19957
Peptide A residue number
83
Peptide B residue number
109
Ligandability
Cysteine 83 of Elafin
Cysteine 109 of Elafin
6atu A 23 I 23
A redox-regulated disulphide may form between two units of Elafin at cysteines 83 and 83 (23 and 23 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
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Elafin
Peptide B name
Elafin
Peptide A accession
P19957
Peptide B accession
P19957
Peptide A residue number
83
Peptide B residue number
83
Ligandability
6atu D 38 D 53
A redox-regulated disulphide may form within Elafin between cysteines 98 and 113 (38 and 53 respectively in this structure).
Details
Redox score ?
87
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
98
Residue number B
113
Peptide name
Elafin
Ligandability
Cysteine 98 of Elafin
Cysteine 113 of Elafin
1fle I 16 I 45
A redox-regulated disulphide may form within Elafin between cysteines 76 and 105 (16 and 45 respectively in this structure).
Details
Redox score ?
85
PDB code
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
76
Residue number B
105
Peptide name
Elafin
Ligandability
Cysteine 76 of Elafin
Cysteine 105 of Elafin
1fle I 32 I 44
A redox-regulated disulphide may form within Elafin between cysteines 92 and 104 (32 and 44 respectively in this structure).
Details
Redox score ?
83
PDB code
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
92
Residue number B
104
Peptide name
Elafin
Ligandability
Cysteine 92 of Elafin
Cysteine 104 of Elafin
6atu A 32 A 38
A redox-regulated disulphide may form within Elafin between cysteines 92 and 98 (32 and 38 respectively in this structure).
Details
Redox score ?
75
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
92
Residue number B
98
Peptide name
Elafin
Ligandability
Cysteine 92 of Elafin
Cysteine 98 of Elafin
6atu H 32 H 53
A redox-regulated disulphide may form within Elafin between cysteines 92 and 113 (32 and 53 respectively in this structure).
Details
Redox score ?
73
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
92
Residue number B
113
Peptide name
Elafin
Ligandability
Cysteine 92 of Elafin
Cysteine 113 of Elafin
6atu N 38 N 44
A redox-regulated disulphide may form within Elafin between cysteines 98 and 104 (38 and 44 respectively in this structure).
Details
Redox score ?
69
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
98
Residue number B
104
Peptide name
Elafin
Ligandability
Cysteine 98 of Elafin
Cysteine 104 of Elafin
6atu M 44 M 53
A redox-regulated disulphide may form within Elafin between cysteines 104 and 113 (44 and 53 respectively in this structure).
Details
Redox score ?
62
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
104
Residue number B
113
Peptide name
Elafin
Ligandability
Cysteine 104 of Elafin
Cysteine 113 of Elafin
6atu J 38 J 45
A redox-regulated disulphide may form within Elafin between cysteines 98 and 105 (38 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
98
Residue number B
105
Peptide name
Elafin
Ligandability
Cysteine 98 of Elafin
Cysteine 105 of Elafin
6atu R 44 R 45
A redox-regulated disulphide may form within Elafin between cysteines 104 and 105 (44 and 45 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
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
104
Residue number B
105
Peptide name
Elafin
Ligandability
Cysteine 104 of Elafin
Cysteine 105 of Elafin
6atu A 32 A 45
A redox-regulated disulphide may form within Elafin between cysteines 92 and 105 (32 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
92
Residue number B
105
Peptide name
Elafin
Ligandability
Cysteine 92 of Elafin
Cysteine 105 of Elafin
6atu H 16 H 44
A redox-regulated disulphide may form within Elafin between cysteines 76 and 104 (16 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
76
Residue number B
104
Peptide name
Elafin
Ligandability
Cysteine 76 of Elafin
Cysteine 104 of Elafin
1fle I 16 I 38
A redox-regulated disulphide may form within Elafin between cysteines 76 and 98 (16 and 38 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
76
Residue number B
98
Peptide name
Elafin
Ligandability
Cysteine 76 of Elafin
Cysteine 98 of Elafin
6atu L 16 L 32
A redox-regulated disulphide may form within Elafin between cysteines 76 and 92 (16 and 32 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
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
76
Residue number B
92
Peptide name
Elafin
Ligandability
Cysteine 76 of Elafin
Cysteine 92 of Elafin
6atu R 45 R 53
A redox-regulated disulphide may form within Elafin between cysteines 105 and 113 (45 and 53 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
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
105
Residue number B
113
Peptide name
Elafin
Ligandability
Cysteine 105 of Elafin
Cysteine 113 of Elafin
6atu Q 16 Q 53
A redox-regulated disulphide may form within Elafin between cysteines 76 and 113 (16 and 53 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
6atu
Structure name
exploring cystine dense peptide space to open a unique molecular toolbox
Structure deposition date
2017-08-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19957
Residue number A
76
Residue number B
113
Peptide name
Elafin
Ligandability
Cysteine 76 of Elafin
Cysteine 113 of Elafin
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