Serine protease hepsin
Intermolecular
Cysteine 153 and cysteine 277
Intramolecular
Cysteine 77 and cysteine 140
Cysteine 90 and cysteine 150
Cysteine 119 and cysteine 138
Cysteine 291 and cysteine 359
Cysteine 322 and cysteine 338
Cysteine 349 and cysteine 381
Cysteine 188 and cysteine 204
Cysteine 138 and cysteine 140
Cysteine 119 and cysteine 140
More...Cysteine 77 and cysteine 138
Cysteine 77 and cysteine 119
Cysteine 359 and cysteine 372
Cysteine 291 and cysteine 372
Cysteine 150 and cysteine 153
Cysteine 90 and cysteine 153
Cysteine 150 and cysteine 277
1o5e L 108 H 122
A redox-regulated disulphide may form between two units of Serine protease hepsin at cysteines 153 and 277 (108 and 122 respectively in this structure).
Details
Redox score ?
80
PDB code
1o5e
Structure name
dissecting and designing inhibitor selectivity determinants at the s1 site using an artificial ala190 protease (ala190 upa)
Structure deposition date
2003-09-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide A name
Serine protease hepsin
Peptide B name
Serine protease hepsin
Peptide A accession
P05981
Peptide B accession
P05981
Peptide A residue number
153
Peptide B residue number
277
Ligandability
Cysteine 153 of Serine protease hepsin
Cysteine 277 of Serine protease hepsin
1o5f L 32 L 95
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 77 and 140 (32 and 95 respectively in this structure).
Details
Redox score ?
84
PDB code
1o5f
Structure name
dissecting and designing inhibitor selectivity determinants at the s1 site using an artificial ala190 protease (ala190 upa)
Structure deposition date
2003-09-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
77
Residue number B
140
Peptide name
Serine protease hepsin
Ligandability
Cysteine 77 of Serine protease hepsin
Cysteine 140 of Serine protease hepsin
1p57 A 45 A 105
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 90 and 150 (45 and 105 respectively in this structure).
Details
Redox score ?
83
PDB code
1p57
Structure name
extracellular domain of human hepsin
Structure deposition date
2003-04-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
90
Residue number B
150
Peptide name
Serine protease hepsin
Ligandability
Cysteine 90 of Serine protease hepsin
Cysteine 150 of Serine protease hepsin
1o5f L 74 L 93
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 119 and 138 (74 and 93 respectively in this structure).
Details
Redox score ?
83
PDB code
1o5f
Structure name
dissecting and designing inhibitor selectivity determinants at the s1 site using an artificial ala190 protease (ala190 upa)
Structure deposition date
2003-09-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
119
Residue number B
138
Peptide name
Serine protease hepsin
Ligandability
Cysteine 119 of Serine protease hepsin
Cysteine 138 of Serine protease hepsin
1o5f H 136 H 201
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 291 and 359 (136 and 201 respectively in this structure).
Details
Redox score ?
82
PDB code
1o5f
Structure name
dissecting and designing inhibitor selectivity determinants at the s1 site using an artificial ala190 protease (ala190 upa)
Structure deposition date
2003-09-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
291
Residue number B
359
Peptide name
Serine protease hepsin
Ligandability
Cysteine 291 of Serine protease hepsin
Cysteine 359 of Serine protease hepsin
5ce1 A 322 A 338
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 322 and 338.
Details
Redox score ?
80
PDB code
5ce1
Structure name
crystal structure of serine protease hepsin in complex with inhibitor
Structure deposition date
2015-07-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
322
Residue number B
338
Peptide name
Serine protease hepsin
Ligandability
Cysteine 322 of Serine protease hepsin
Cysteine 338 of Serine protease hepsin
1o5e H 191 H 220
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 349 and 381 (191 and 220 respectively in this structure).
Details
Redox score ?
80
PDB code
1o5e
Structure name
dissecting and designing inhibitor selectivity determinants at the s1 site using an artificial ala190 protease (ala190 upa)
Structure deposition date
2003-09-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
349
Residue number B
381
Peptide name
Serine protease hepsin
Ligandability
Cysteine 349 of Serine protease hepsin
Cysteine 381 of Serine protease hepsin
1o5e H 42 H 58
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 188 and 204 (42 and 58 respectively in this structure).
Details
Redox score ?
79
PDB code
1o5e
Structure name
dissecting and designing inhibitor selectivity determinants at the s1 site using an artificial ala190 protease (ala190 upa)
Structure deposition date
2003-09-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
188
Residue number B
204
Peptide name
Serine protease hepsin
Ligandability
Cysteine 188 of Serine protease hepsin
Cysteine 204 of Serine protease hepsin
3t2n B 138 B 140
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 138 and 140.
Details
Redox score ?
78
PDB code
3t2n
Structure name
human hepsin protease in complex with the fab fragment of an inhibitory antibody
Structure deposition date
2011-07-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
138
Residue number B
140
Peptide name
Serine protease hepsin
Ligandability
Cysteine 138 of Serine protease hepsin
Cysteine 140 of Serine protease hepsin
3t2n B 119 B 140
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 119 and 140.
Details
Redox score ?
71
PDB code
3t2n
Structure name
human hepsin protease in complex with the fab fragment of an inhibitory antibody
Structure deposition date
2011-07-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
119
Residue number B
140
Peptide name
Serine protease hepsin
Ligandability
Cysteine 119 of Serine protease hepsin
Cysteine 140 of Serine protease hepsin
3t2n A 77 A 138
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 77 and 138.
Details
Redox score ?
68
PDB code
3t2n
Structure name
human hepsin protease in complex with the fab fragment of an inhibitory antibody
Structure deposition date
2011-07-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
77
Residue number B
138
Peptide name
Serine protease hepsin
Ligandability
Cysteine 77 of Serine protease hepsin
Cysteine 138 of Serine protease hepsin
1o5f L 32 L 74
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 77 and 119 (32 and 74 respectively in this structure).
Details
Redox score ?
67
PDB code
1o5f
Structure name
dissecting and designing inhibitor selectivity determinants at the s1 site using an artificial ala190 protease (ala190 upa)
Structure deposition date
2003-09-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
77
Residue number B
119
Peptide name
Serine protease hepsin
Ligandability
Cysteine 77 of Serine protease hepsin
Cysteine 119 of Serine protease hepsin
3t2n B 359 B 372
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 359 and 372.
Details
Redox score ?
66
PDB code
3t2n
Structure name
human hepsin protease in complex with the fab fragment of an inhibitory antibody
Structure deposition date
2011-07-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
nan
Peptide accession
P05981
Residue number A
359
Residue number B
372
Peptide name
Serine protease hepsin
Ligandability
Cysteine 359 of Serine protease hepsin
Cysteine 372 of Serine protease hepsin
3t2n A 291 A 372
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 291 and 372. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
3t2n
Structure name
human hepsin protease in complex with the fab fragment of an inhibitory antibody
Structure deposition date
2011-07-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
nan
Peptide accession
P05981
Residue number A
291
Residue number B
372
Peptide name
Serine protease hepsin
Ligandability
Cysteine 291 of Serine protease hepsin
Cysteine 372 of Serine protease hepsin
1p57 A 105 A 108
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 150 and 153 (105 and 108 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
1p57
Structure name
extracellular domain of human hepsin
Structure deposition date
2003-04-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
150
Residue number B
153
Peptide name
Serine protease hepsin
Ligandability
Cysteine 150 of Serine protease hepsin
Cysteine 153 of Serine protease hepsin
5ce1 A 90 A 153
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 90 and 153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5ce1
Structure name
crystal structure of serine protease hepsin in complex with inhibitor
Structure deposition date
2015-07-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
90
Residue number B
153
Peptide name
Serine protease hepsin
Ligandability
Cysteine 90 of Serine protease hepsin
Cysteine 153 of Serine protease hepsin
3t2n A 150 A 277
A redox-regulated disulphide may form within Serine protease hepsin between cysteines 150 and 277. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3t2n
Structure name
human hepsin protease in complex with the fab fragment of an inhibitory antibody
Structure deposition date
2011-07-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05981
Residue number A
150
Residue number B
277
Peptide name
Serine protease hepsin
Ligandability
Cysteine 150 of Serine protease hepsin
Cysteine 277 of Serine protease hepsin
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