Enteropeptidase
Intermolecular
Cysteine 772 and cysteine 896
Intramolecular
Cysteine 191 and cysteine 210
Cysteine 650 and cysteine 668
Cysteine 184 and cysteine 197
Cysteine 347 and cysteine 354
Cysteine 422 and cysteine 502
Cysteine 716 and cysteine 767
Cysteine 225 and cysteine 253
Cysteine 662 and cysteine 677
Cysteine 204 and cysteine 221
More...Cysteine 910 and cysteine 977
Cysteine 967 and cysteine 995
Cysteine 810 and cysteine 826
Cysteine 703 and cysteine 757
Cysteine 941 and cysteine 956
Cysteine 643 and cysteine 655
Cysteine 524 and cysteine 552
Cysteine 184 and cysteine 191
Cysteine 191 and cysteine 197
Cysteine 650 and cysteine 655
Cysteine 655 and cysteine 668
Cysteine 184 and cysteine 210
Cysteine 643 and cysteine 650
Cysteine 668 and cysteine 677
Cysteine 210 and cysteine 221
Cysteine 662 and cysteine 668
Cysteine 197 and cysteine 210
8h3s A 772 B 896
A redox-regulated disulphide may form between two units of Enteropeptidase at cysteines 772 and 896.
Details
Redox score ?
81
PDB code
8h3s
Structure name
substrate-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Enteropeptidase
Peptide B name
Enteropeptidase
Peptide A accession
P98073
Peptide B accession
P98073
Peptide A residue number
772
Peptide B residue number
896
Ligandability
Cysteine 772 of Enteropeptidase
Cysteine 896 of Enteropeptidase
8h3u A 191 A 210
A redox-regulated disulphide may form within Enteropeptidase between cysteines 191 and 210.
Details
Redox score ?
88
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
191
Residue number B
210
Peptide name
Enteropeptidase
Ligandability
Cysteine 191 of Enteropeptidase
Cysteine 210 of Enteropeptidase
7wr7 A 650 A 668
A redox-regulated disulphide may form within Enteropeptidase between cysteines 650 and 668.
Details
Redox score ?
88
PDB code
7wr7
Structure name
structure of inhibited-ep
Structure deposition date
2022-01-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
650
Residue number B
668
Peptide name
Enteropeptidase
Ligandability
Cysteine 650 of Enteropeptidase
Cysteine 668 of Enteropeptidase
8h3u A 184 A 197
A redox-regulated disulphide may form within Enteropeptidase between cysteines 184 and 197.
Details
Redox score ?
88
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
184
Residue number B
197
Peptide name
Enteropeptidase
Ligandability
Cysteine 184 of Enteropeptidase
Cysteine 197 of Enteropeptidase
8h3s A 347 A 354
A redox-regulated disulphide may form within Enteropeptidase between cysteines 347 and 354.
Details
Redox score ?
87
PDB code
8h3s
Structure name
substrate-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
347
Residue number B
354
Peptide name
Enteropeptidase
Ligandability
Cysteine 347 of Enteropeptidase
Cysteine 354 of Enteropeptidase
8h3u A 422 A 502
A redox-regulated disulphide may form within Enteropeptidase between cysteines 422 and 502.
Details
Redox score ?
86
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
422
Residue number B
502
Peptide name
Enteropeptidase
Ligandability
Cysteine 422 of Enteropeptidase
Cysteine 502 of Enteropeptidase
7wqz A 716 A 767
A redox-regulated disulphide may form within Enteropeptidase between cysteines 716 and 767.
Details
Redox score ?
85
PDB code
7wqz
Structure name
structure of active-mutep
Structure deposition date
2022-01-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
716
Residue number B
767
Peptide name
Enteropeptidase
Ligandability
Cysteine 716 of Enteropeptidase
Cysteine 767 of Enteropeptidase
8h3u A 225 A 253
A redox-regulated disulphide may form within Enteropeptidase between cysteines 225 and 253.
Details
Redox score ?
85
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
225
Residue number B
253
Peptide name
Enteropeptidase
Ligandability
Cysteine 225 of Enteropeptidase
Cysteine 253 of Enteropeptidase
7wqx A 662 A 677
A redox-regulated disulphide may form within Enteropeptidase between cysteines 662 and 677.
Details
Redox score ?
85
PDB code
7wqx
Structure name
structure of inactive-ep
Structure deposition date
2022-01-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
662
Residue number B
677
Peptide name
Enteropeptidase
Ligandability
Cysteine 662 of Enteropeptidase
Cysteine 677 of Enteropeptidase
8h3u A 204 A 221
A redox-regulated disulphide may form within Enteropeptidase between cysteines 204 and 221.
Details
Redox score ?
84
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
204
Residue number B
221
Peptide name
Enteropeptidase
Ligandability
Cysteine 204 of Enteropeptidase
Cysteine 221 of Enteropeptidase
4dgj D 126 D 193
A redox-regulated disulphide may form within Enteropeptidase between cysteines 910 and 977 (126 and 193 respectively in this structure).
Details
Redox score ?
83
PDB code
4dgj
Structure name
structure of a human enteropeptidase light chain variant
Structure deposition date
2012-01-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
910
Residue number B
977
Peptide name
Enteropeptidase
Ligandability
Cysteine 910 of Enteropeptidase
Cysteine 977 of Enteropeptidase
4dgj A 183 A 211
A redox-regulated disulphide may form within Enteropeptidase between cysteines 967 and 995 (183 and 211 respectively in this structure).
Details
Redox score ?
80
PDB code
4dgj
Structure name
structure of a human enteropeptidase light chain variant
Structure deposition date
2012-01-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
967
Residue number B
995
Peptide name
Enteropeptidase
Ligandability
Cysteine 967 of Enteropeptidase
Cysteine 995 of Enteropeptidase
4dgj B 26 B 42
A redox-regulated disulphide may form within Enteropeptidase between cysteines 810 and 826 (26 and 42 respectively in this structure).
Details
Redox score ?
80
PDB code
4dgj
Structure name
structure of a human enteropeptidase light chain variant
Structure deposition date
2012-01-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
810
Residue number B
826
Peptide name
Enteropeptidase
Ligandability
Cysteine 810 of Enteropeptidase
Cysteine 826 of Enteropeptidase
8h3u A 703 A 757
A redox-regulated disulphide may form within Enteropeptidase between cysteines 703 and 757.
Details
Redox score ?
79
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
15
Peptide accession
P98073
Residue number A
703
Residue number B
757
Peptide name
Enteropeptidase
Ligandability
Cysteine 703 of Enteropeptidase
Cysteine 757 of Enteropeptidase
4dgj A 157 A 172
A redox-regulated disulphide may form within Enteropeptidase between cysteines 941 and 956 (157 and 172 respectively in this structure).
Details
Redox score ?
79
PDB code
4dgj
Structure name
structure of a human enteropeptidase light chain variant
Structure deposition date
2012-01-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
941
Residue number B
956
Peptide name
Enteropeptidase
Ligandability
Cysteine 941 of Enteropeptidase
Cysteine 956 of Enteropeptidase
7wqw A 643 A 655
A redox-regulated disulphide may form within Enteropeptidase between cysteines 643 and 655.
Details
Redox score ?
65
PDB code
7wqw
Structure name
structure of active-ep
Structure deposition date
2022-01-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
0
Peptide accession
P98073
Residue number A
643
Residue number B
655
Peptide name
Enteropeptidase
Ligandability
Cysteine 643 of Enteropeptidase
Cysteine 655 of Enteropeptidase
7wqw A 524 A 552
A redox-regulated disulphide may form within Enteropeptidase between cysteines 524 and 552. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
7wqw
Structure name
structure of active-ep
Structure deposition date
2022-01-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
nan
Peptide accession
P98073
Residue number A
524
Residue number B
552
Peptide name
Enteropeptidase
Ligandability
Cysteine 524 of Enteropeptidase
Cysteine 552 of Enteropeptidase
8h3u A 184 A 191
A redox-regulated disulphide may form within Enteropeptidase between cysteines 184 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
184
Residue number B
191
Peptide name
Enteropeptidase
Ligandability
Cysteine 184 of Enteropeptidase
Cysteine 191 of Enteropeptidase
8h3u A 191 A 197
A redox-regulated disulphide may form within Enteropeptidase between cysteines 191 and 197. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
191
Residue number B
197
Peptide name
Enteropeptidase
Ligandability
Cysteine 191 of Enteropeptidase
Cysteine 197 of Enteropeptidase
8h3s A 650 A 655
A redox-regulated disulphide may form within Enteropeptidase between cysteines 650 and 655. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
8h3s
Structure name
substrate-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
nan
Peptide accession
P98073
Residue number A
650
Residue number B
655
Peptide name
Enteropeptidase
Ligandability
Cysteine 650 of Enteropeptidase
Cysteine 655 of Enteropeptidase
8h3s A 655 A 668
A redox-regulated disulphide may form within Enteropeptidase between cysteines 655 and 668. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
8h3s
Structure name
substrate-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
nan
Peptide accession
P98073
Residue number A
655
Residue number B
668
Peptide name
Enteropeptidase
Ligandability
Cysteine 655 of Enteropeptidase
Cysteine 668 of Enteropeptidase
8h3u A 184 A 210
A redox-regulated disulphide may form within Enteropeptidase between cysteines 184 and 210. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
184
Residue number B
210
Peptide name
Enteropeptidase
Ligandability
Cysteine 184 of Enteropeptidase
Cysteine 210 of Enteropeptidase
7wqx A 643 A 650
A redox-regulated disulphide may form within Enteropeptidase between cysteines 643 and 650. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
7wqx
Structure name
structure of inactive-ep
Structure deposition date
2022-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
643
Residue number B
650
Peptide name
Enteropeptidase
Ligandability
Cysteine 643 of Enteropeptidase
Cysteine 650 of Enteropeptidase
7wqx A 668 A 677
A redox-regulated disulphide may form within Enteropeptidase between cysteines 668 and 677. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7wqx
Structure name
structure of inactive-ep
Structure deposition date
2022-01-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
668
Residue number B
677
Peptide name
Enteropeptidase
Ligandability
Cysteine 668 of Enteropeptidase
Cysteine 677 of Enteropeptidase
8h3u A 210 A 221
A redox-regulated disulphide may form within Enteropeptidase between cysteines 210 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
210
Residue number B
221
Peptide name
Enteropeptidase
Ligandability
Cysteine 210 of Enteropeptidase
Cysteine 221 of Enteropeptidase
7wqx A 662 A 668
A redox-regulated disulphide may form within Enteropeptidase between cysteines 662 and 668. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7wqx
Structure name
structure of inactive-ep
Structure deposition date
2022-01-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
662
Residue number B
668
Peptide name
Enteropeptidase
Ligandability
Cysteine 662 of Enteropeptidase
Cysteine 668 of Enteropeptidase
8h3u A 197 A 210
A redox-regulated disulphide may form within Enteropeptidase between cysteines 197 and 210. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
8h3u
Structure name
inhibitor-bound ep, polya model
Structure deposition date
2022-10-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P98073
Residue number A
197
Residue number B
210
Peptide name
Enteropeptidase
Ligandability
Cysteine 197 of Enteropeptidase
Cysteine 210 of Enteropeptidase
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