Kunitz-type protease inhibitor 1
Intermolecular
Cysteine 448 of Hepatocyte growth factor activator and cysteine 259
Cysteine 657 of Suppressor of tumorigenicity 14 protein and cysteine 283
Cysteine 657 of Suppressor of tumorigenicity 14 protein and cysteine 259
Cysteine 448 of Hepatocyte growth factor activator and cysteine 283
Cysteine 283 and cysteine 641 of Suppressor of tumorigenicity 14 protein
Cysteine 432 of Hepatocyte growth factor activator and cysteine 259
Cysteine 259 and cysteine 641 of Suppressor of tumorigenicity 14 protein
Intramolecular
Cysteine 391 and cysteine 441
Cysteine 416 and cysteine 437
Cysteine 275 and cysteine 296
More...Cysteine 91 and cysteine 97
Cysteine 50 and cysteine 92
Cysteine 259 and cysteine 283
Cysteine 400 and cysteine 424
Cysteine 87 and cysteine 116
Cysteine 121 and cysteine 129
Cysteine 250 and cysteine 300
Cysteine 437 and cysteine 441
Cysteine 296 and cysteine 300
Cysteine 416 and cysteine 441
Cysteine 275 and cysteine 300
Cysteine 391 and cysteine 437
Cysteine 91 and cysteine 92
Cysteine 250 and cysteine 296
Cysteine 87 and cysteine 91
Cysteine 87 and cysteine 97
Cysteine 50 and cysteine 91
Cysteine 250 and cysteine 275
Cysteine 391 and cysteine 416
Cysteine 97 and cysteine 116
Cysteine 91 and cysteine 116
Cysteine 92 and cysteine 97
Cysteine 50 and cysteine 97
Cysteine 91 and cysteine 121
Cysteine 97 and cysteine 121
1yc0 A 448 I 259
A redox-regulated disulphide may form between cysteine 448 of Hepatocyte growth factor activator and cysteine 259 of Kunitz-type protease inhibitor 1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1yc0
Structure name
short form hgfa with first kunitz domain from hai-1
Structure deposition date
2004-12-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepatocyte growth factor activator
Peptide B name
Kunitz-type protease inhibitor 1
Peptide A accession
Q04756
Peptide B accession
O43278
Peptide A residue number
448
Peptide B residue number
259
Ligandability
Cysteine 448 of Hepatocyte growth factor activator
Cysteine 259 of Kunitz-type protease inhibitor 1
4iso A 58 B 283
A redox-regulated disulphide may form between cysteine 657 of Suppressor of tumorigenicity 14 protein and cysteine 283 of Kunitz-type protease inhibitor 1 (58 and 283 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
4iso
Structure name
crystal structure of matriptase in complex with its inhibitor hai-1
Structure deposition date
2013-01-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide A name
Suppressor of tumorigenicity 14 protein
Peptide B name
Kunitz-type protease inhibitor 1
Peptide A accession
Q9Y5Y6
Peptide B accession
O43278
Peptide A residue number
657
Peptide B residue number
283
Ligandability
Cysteine 657 of Suppressor of tumorigenicity 14 protein
Cysteine 283 of Kunitz-type protease inhibitor 1
4iso A 58 B 259
A redox-regulated disulphide may form between cysteine 657 of Suppressor of tumorigenicity 14 protein and cysteine 259 of Kunitz-type protease inhibitor 1 (58 and 259 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
4iso
Structure name
crystal structure of matriptase in complex with its inhibitor hai-1
Structure deposition date
2013-01-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide A name
Suppressor of tumorigenicity 14 protein
Peptide B name
Kunitz-type protease inhibitor 1
Peptide A accession
Q9Y5Y6
Peptide B accession
O43278
Peptide A residue number
657
Peptide B residue number
259
Ligandability
Cysteine 657 of Suppressor of tumorigenicity 14 protein
Cysteine 259 of Kunitz-type protease inhibitor 1
1yc0 A 448 I 283
A redox-regulated disulphide may form between cysteine 448 of Hepatocyte growth factor activator and cysteine 283 of Kunitz-type protease inhibitor 1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1yc0
Structure name
short form hgfa with first kunitz domain from hai-1
Structure deposition date
2004-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepatocyte growth factor activator
Peptide B name
Kunitz-type protease inhibitor 1
Peptide A accession
Q04756
Peptide B accession
O43278
Peptide A residue number
448
Peptide B residue number
283
Ligandability
Cysteine 448 of Hepatocyte growth factor activator
Cysteine 283 of Kunitz-type protease inhibitor 1
4isl B 283 A 42
A redox-regulated disulphide may form between cysteine 283 of Kunitz-type protease inhibitor 1 and cysteine 641 of Suppressor of tumorigenicity 14 protein (283 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 ?
38
PDB code
4isl
Structure name
crystal structure of the inactive matriptase in complex with its inhibitor hai-1
Structure deposition date
2013-01-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide A name
Kunitz-type protease inhibitor 1
Peptide B name
Suppressor of tumorigenicity 14 protein
Peptide A accession
O43278
Peptide B accession
Q9Y5Y6
Peptide A residue number
283
Peptide B residue number
641
Ligandability
Cysteine 283 of Kunitz-type protease inhibitor 1
Cysteine 641 of Suppressor of tumorigenicity 14 protein
1yc0 A 432 I 259
A redox-regulated disulphide may form between cysteine 432 of Hepatocyte growth factor activator and cysteine 259 of Kunitz-type protease inhibitor 1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
1yc0
Structure name
short form hgfa with first kunitz domain from hai-1
Structure deposition date
2004-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepatocyte growth factor activator
Peptide B name
Kunitz-type protease inhibitor 1
Peptide A accession
Q04756
Peptide B accession
O43278
Peptide A residue number
432
Peptide B residue number
259
Ligandability
Cysteine 432 of Hepatocyte growth factor activator
Cysteine 259 of Kunitz-type protease inhibitor 1
4isl B 259 A 42
A redox-regulated disulphide may form between cysteine 259 of Kunitz-type protease inhibitor 1 and cysteine 641 of Suppressor of tumorigenicity 14 protein (259 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 ?
36
PDB code
4isl
Structure name
crystal structure of the inactive matriptase in complex with its inhibitor hai-1
Structure deposition date
2013-01-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide A name
Kunitz-type protease inhibitor 1
Peptide B name
Suppressor of tumorigenicity 14 protein
Peptide A accession
O43278
Peptide B accession
Q9Y5Y6
Peptide A residue number
259
Peptide B residue number
641
Ligandability
Cysteine 259 of Kunitz-type protease inhibitor 1
Cysteine 641 of Suppressor of tumorigenicity 14 protein
5h7v A 375 A 425
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 391 and 441 (375 and 425 respectively in this structure).
Details
Redox score ?
90
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
391
Residue number B
441
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 391 of Kunitz-type protease inhibitor 1
Cysteine 441 of Kunitz-type protease inhibitor 1
5h7v A 400 A 421
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 416 and 437 (400 and 421 respectively in this structure).
Details
Redox score ?
88
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
416
Residue number B
437
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 416 of Kunitz-type protease inhibitor 1
Cysteine 437 of Kunitz-type protease inhibitor 1
4isl B 275 B 296
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 275 and 296.
Details
Redox score ?
86
PDB code
4isl
Structure name
crystal structure of the inactive matriptase in complex with its inhibitor hai-1
Structure deposition date
2013-01-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
275
Residue number B
296
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 275 of Kunitz-type protease inhibitor 1
Cysteine 296 of Kunitz-type protease inhibitor 1
5h7v A 91 A 97
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 91 and 97.
Details
Redox score ?
85
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
91
Residue number B
97
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 91 of Kunitz-type protease inhibitor 1
Cysteine 97 of Kunitz-type protease inhibitor 1
5h7v A 50 A 92
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 50 and 92.
Details
Redox score ?
84
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
50
Residue number B
92
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 50 of Kunitz-type protease inhibitor 1
Cysteine 92 of Kunitz-type protease inhibitor 1
5h7v A 259 A 283
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 259 and 283.
Details
Redox score ?
84
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
259
Residue number B
283
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 259 of Kunitz-type protease inhibitor 1
Cysteine 283 of Kunitz-type protease inhibitor 1
5h7v A 384 A 408
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 400 and 424 (384 and 408 respectively in this structure).
Details
Redox score ?
84
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
400
Residue number B
424
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 400 of Kunitz-type protease inhibitor 1
Cysteine 424 of Kunitz-type protease inhibitor 1
5h7v A 87 A 116
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 87 and 116.
Details
Redox score ?
83
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
87
Residue number B
116
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 87 of Kunitz-type protease inhibitor 1
Cysteine 116 of Kunitz-type protease inhibitor 1
5h7v A 121 A 129
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 121 and 129.
Details
Redox score ?
83
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
121
Residue number B
129
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 121 of Kunitz-type protease inhibitor 1
Cysteine 129 of Kunitz-type protease inhibitor 1
5ezd B 250 B 300
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 250 and 300.
Details
Redox score ?
82
PDB code
5ezd
Structure name
crystal structure of a hepatocyte growth factor activator inhibitor-1 (hai-1) fragment covering the pkd-like 'internal' domain and kunitz domain 1
Structure deposition date
2015-11-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
250
Residue number B
300
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 250 of Kunitz-type protease inhibitor 1
Cysteine 300 of Kunitz-type protease inhibitor 1
5h7v A 421 A 425
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 437 and 441 (421 and 425 respectively in this structure).
Details
Redox score ?
71
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
437
Residue number B
441
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 437 of Kunitz-type protease inhibitor 1
Cysteine 441 of Kunitz-type protease inhibitor 1
5ezd B 296 B 300
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 296 and 300.
Details
Redox score ?
66
PDB code
5ezd
Structure name
crystal structure of a hepatocyte growth factor activator inhibitor-1 (hai-1) fragment covering the pkd-like 'internal' domain and kunitz domain 1
Structure deposition date
2015-11-26
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
296
Residue number B
300
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 296 of Kunitz-type protease inhibitor 1
Cysteine 300 of Kunitz-type protease inhibitor 1
5h7v A 400 A 425
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 416 and 441 (400 and 425 respectively in this structure).
Details
Redox score ?
64
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
416
Residue number B
441
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 416 of Kunitz-type protease inhibitor 1
Cysteine 441 of Kunitz-type protease inhibitor 1
5ezd B 275 B 300
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 275 and 300.
Details
Redox score ?
62
PDB code
5ezd
Structure name
crystal structure of a hepatocyte growth factor activator inhibitor-1 (hai-1) fragment covering the pkd-like 'internal' domain and kunitz domain 1
Structure deposition date
2015-11-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
275
Residue number B
300
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 275 of Kunitz-type protease inhibitor 1
Cysteine 300 of Kunitz-type protease inhibitor 1
5h7v A 375 A 421
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 391 and 437 (375 and 421 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
391
Residue number B
437
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 391 of Kunitz-type protease inhibitor 1
Cysteine 437 of Kunitz-type protease inhibitor 1
5h7v A 91 A 92
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 91 and 92. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
91
Residue number B
92
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 91 of Kunitz-type protease inhibitor 1
Cysteine 92 of Kunitz-type protease inhibitor 1
4iso B 250 B 296
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 250 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
4iso
Structure name
crystal structure of matriptase in complex with its inhibitor hai-1
Structure deposition date
2013-01-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
250
Residue number B
296
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 250 of Kunitz-type protease inhibitor 1
Cysteine 296 of Kunitz-type protease inhibitor 1
5h7v A 87 A 91
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 87 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
87
Residue number B
91
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 87 of Kunitz-type protease inhibitor 1
Cysteine 91 of Kunitz-type protease inhibitor 1
5h7v A 87 A 97
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 87 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
87
Residue number B
97
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 87 of Kunitz-type protease inhibitor 1
Cysteine 97 of Kunitz-type protease inhibitor 1
5h7v A 50 A 91
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 50 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
50
Residue number B
91
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 50 of Kunitz-type protease inhibitor 1
Cysteine 91 of Kunitz-type protease inhibitor 1
5ezd A 250 A 275
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 250 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5ezd
Structure name
crystal structure of a hepatocyte growth factor activator inhibitor-1 (hai-1) fragment covering the pkd-like 'internal' domain and kunitz domain 1
Structure deposition date
2015-11-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
250
Residue number B
275
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 250 of Kunitz-type protease inhibitor 1
Cysteine 275 of Kunitz-type protease inhibitor 1
5h7v A 375 A 400
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 391 and 416 (375 and 400 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
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
391
Residue number B
416
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 391 of Kunitz-type protease inhibitor 1
Cysteine 416 of Kunitz-type protease inhibitor 1
5h7v A 97 A 116
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 97 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
97
Residue number B
116
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 97 of Kunitz-type protease inhibitor 1
Cysteine 116 of Kunitz-type protease inhibitor 1
5h7v A 91 A 116
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 91 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
91
Residue number B
116
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 91 of Kunitz-type protease inhibitor 1
Cysteine 116 of Kunitz-type protease inhibitor 1
5h7v A 92 A 97
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 92 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
92
Residue number B
97
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 92 of Kunitz-type protease inhibitor 1
Cysteine 97 of Kunitz-type protease inhibitor 1
5h7v A 50 A 97
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 50 and 97. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5h7v
Structure name
structure of full-length extracellular domain of hai-1 at ph 4
Structure deposition date
2016-11-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
50
Residue number B
97
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 50 of Kunitz-type protease inhibitor 1
Cysteine 97 of Kunitz-type protease inhibitor 1
2msx A 91 A 121
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 91 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
2msx
Structure name
the solution structure of the manec-type domain from hepatocyte growth factor inhibitor 1 reveals an unexpected pan/apple domain-type fold
Structure deposition date
2014-08-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
91
Residue number B
121
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 91 of Kunitz-type protease inhibitor 1
Cysteine 121 of Kunitz-type protease inhibitor 1
2msx A 97 A 121
A redox-regulated disulphide may form within Kunitz-type protease inhibitor 1 between cysteines 97 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
2msx
Structure name
the solution structure of the manec-type domain from hepatocyte growth factor inhibitor 1 reveals an unexpected pan/apple domain-type fold
Structure deposition date
2014-08-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O43278
Residue number A
97
Residue number B
121
Peptide name
Kunitz-type protease inhibitor 1
Ligandability
Cysteine 97 of Kunitz-type protease inhibitor 1
Cysteine 121 of Kunitz-type protease inhibitor 1
If this tool was useful for finding a disulphide, please cite: