Serine protease inhibitor Kazal-type 5
Intramolecular
Cysteine 44 and cysteine 63
Cysteine 1014 and cysteine 1046
Cysteine 993 and cysteine 1028
Cysteine 1006 and cysteine 1025
Cysteine 381 and cysteine 400
Cysteine 30 and cysteine 66
Cysteine 367 and cysteine 403
Cysteine 30 and cysteine 44
Cysteine 63 and cysteine 66
Cysteine 993 and cysteine 1025
More...Cysteine 400 and cysteine 403
Cysteine 1025 and cysteine 1028
Cysteine 1006 and cysteine 1028
Cysteine 993 and cysteine 1006
Cysteine 44 and cysteine 66
Cysteine 367 and cysteine 400
Cysteine 381 and cysteine 403
Cysteine 367 and cysteine 381
Cysteine 30 and cysteine 63
1hdl A 22 A 41
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 44 and 63 (22 and 41 respectively in this structure).
Details
Redox score ?
87
PDB code
1hdl
Structure name
lekti domain one
Structure deposition date
2000-11-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
44
Residue number B
63
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 44 of Serine protease inhibitor Kazal-type 5
Cysteine 63 of Serine protease inhibitor Kazal-type 5
1uvf A 26 A 58
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 1014 and 1046 (26 and 58 respectively in this structure).
Details
Redox score ?
86
PDB code
1uvf
Structure name
solution structure of the structured part of the 15th domain of lekti
Structure deposition date
2004-01-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
1014
Residue number B
1046
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 1014 of Serine protease inhibitor Kazal-type 5
Cysteine 1046 of Serine protease inhibitor Kazal-type 5
1uvf A 5 A 40
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 993 and 1028 (5 and 40 respectively in this structure).
Details
Redox score ?
85
PDB code
1uvf
Structure name
solution structure of the structured part of the 15th domain of lekti
Structure deposition date
2004-01-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
993
Residue number B
1028
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 993 of Serine protease inhibitor Kazal-type 5
Cysteine 1028 of Serine protease inhibitor Kazal-type 5
1uvg A 18 A 37
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 1006 and 1025 (18 and 37 respectively in this structure).
Details
Redox score ?
84
PDB code
1uvg
Structure name
solution structure of the 15th domain of lekti
Structure deposition date
2004-01-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
1006
Residue number B
1025
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 1006 of Serine protease inhibitor Kazal-type 5
Cysteine 1025 of Serine protease inhibitor Kazal-type 5
1h0z A 26 A 45
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 381 and 400 (26 and 45 respectively in this structure).
Details
Redox score ?
84
PDB code
1h0z
Structure name
lekti domain six
Structure deposition date
2002-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
381
Residue number B
400
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 381 of Serine protease inhibitor Kazal-type 5
Cysteine 400 of Serine protease inhibitor Kazal-type 5
1uuc A 8 A 44
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 30 and 66 (8 and 44 respectively in this structure).
Details
Redox score ?
84
PDB code
1uuc
Structure name
solution structure of a chimeric lekti-domain
Structure deposition date
2003-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
30
Residue number B
66
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 30 of Serine protease inhibitor Kazal-type 5
Cysteine 66 of Serine protease inhibitor Kazal-type 5
1h0z A 12 A 48
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 367 and 403 (12 and 48 respectively in this structure).
Details
Redox score ?
83
PDB code
1h0z
Structure name
lekti domain six
Structure deposition date
2002-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
367
Residue number B
403
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 367 of Serine protease inhibitor Kazal-type 5
Cysteine 403 of Serine protease inhibitor Kazal-type 5
1hdl A 8 A 22
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 30 and 44 (8 and 22 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
1hdl
Structure name
lekti domain one
Structure deposition date
2000-11-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
30
Residue number B
44
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 30 of Serine protease inhibitor Kazal-type 5
Cysteine 44 of Serine protease inhibitor Kazal-type 5
1hdl A 41 A 44
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 63 and 66 (41 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 ?
54
PDB code
1hdl
Structure name
lekti domain one
Structure deposition date
2000-11-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
63
Residue number B
66
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 63 of Serine protease inhibitor Kazal-type 5
Cysteine 66 of Serine protease inhibitor Kazal-type 5
1uvg A 5 A 37
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 993 and 1025 (5 and 37 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
1uvg
Structure name
solution structure of the 15th domain of lekti
Structure deposition date
2004-01-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
993
Residue number B
1025
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 993 of Serine protease inhibitor Kazal-type 5
Cysteine 1025 of Serine protease inhibitor Kazal-type 5
1h0z A 45 A 48
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 400 and 403 (45 and 48 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
1h0z
Structure name
lekti domain six
Structure deposition date
2002-07-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
400
Residue number B
403
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 400 of Serine protease inhibitor Kazal-type 5
Cysteine 403 of Serine protease inhibitor Kazal-type 5
1uvf A 37 A 40
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 1025 and 1028 (37 and 40 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
1uvf
Structure name
solution structure of the structured part of the 15th domain of lekti
Structure deposition date
2004-01-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
1025
Residue number B
1028
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 1025 of Serine protease inhibitor Kazal-type 5
Cysteine 1028 of Serine protease inhibitor Kazal-type 5
1uvg A 18 A 40
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 1006 and 1028 (18 and 40 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
1uvg
Structure name
solution structure of the 15th domain of lekti
Structure deposition date
2004-01-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
1006
Residue number B
1028
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 1006 of Serine protease inhibitor Kazal-type 5
Cysteine 1028 of Serine protease inhibitor Kazal-type 5
1uvf A 5 A 18
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 993 and 1006 (5 and 18 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
1uvf
Structure name
solution structure of the structured part of the 15th domain of lekti
Structure deposition date
2004-01-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
993
Residue number B
1006
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 993 of Serine protease inhibitor Kazal-type 5
Cysteine 1006 of Serine protease inhibitor Kazal-type 5
1uuc A 22 A 44
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 44 and 66 (22 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 ?
47
PDB code
1uuc
Structure name
solution structure of a chimeric lekti-domain
Structure deposition date
2003-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
44
Residue number B
66
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 44 of Serine protease inhibitor Kazal-type 5
Cysteine 66 of Serine protease inhibitor Kazal-type 5
1h0z A 12 A 45
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 367 and 400 (12 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 ?
46
PDB code
1h0z
Structure name
lekti domain six
Structure deposition date
2002-07-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
367
Residue number B
400
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 367 of Serine protease inhibitor Kazal-type 5
Cysteine 400 of Serine protease inhibitor Kazal-type 5
1h0z A 26 A 48
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 381 and 403 (26 and 48 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
1h0z
Structure name
lekti domain six
Structure deposition date
2002-07-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
381
Residue number B
403
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 381 of Serine protease inhibitor Kazal-type 5
Cysteine 403 of Serine protease inhibitor Kazal-type 5
1h0z A 12 A 26
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 367 and 381 (12 and 26 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
1h0z
Structure name
lekti domain six
Structure deposition date
2002-07-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
367
Residue number B
381
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 367 of Serine protease inhibitor Kazal-type 5
Cysteine 381 of Serine protease inhibitor Kazal-type 5
1uuc A 8 A 41
A redox-regulated disulphide may form within Serine protease inhibitor Kazal-type 5 between cysteines 30 and 63 (8 and 41 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
1uuc
Structure name
solution structure of a chimeric lekti-domain
Structure deposition date
2003-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NQ38
Residue number A
30
Residue number B
63
Peptide name
Serine protease inhibitor Kazal-type 5
Ligandability
Cysteine 30 of Serine protease inhibitor Kazal-type 5
Cysteine 63 of Serine protease inhibitor Kazal-type 5
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