Pancreatic trypsin inhibitor
Intermolecular
Cysteine 40 and cysteine 90
Cysteine 86 of Prostasin and cysteine 49
Cysteine 121 of Trypsin-3 and cysteine 49
Cysteine 657 of Suppressor of tumorigenicity 14 protein and cysteine 49
Cysteine 49 of Glandular kallikrein and cysteine 49
Cysteine 68 of PRSS3 protein and cysteine 49
Cysteine 46 of Hepatopancreas trypsin and cysteine 49
Cysteine 254 of Coagulation factor VII and cysteine 49
Cysteine 105 of Trypsin-3 and cysteine 49
Cysteine 52 of PRSS3 protein and cysteine 49
More...Cysteine 238 of Coagulation factor VII and cysteine 49
Cysteine 641 of Suppressor of tumorigenicity 14 protein and cysteine 49
Cysteine 30 of Hepatopancreas trypsin and cysteine 49
Cysteine 33 of Glandular kallikrein and cysteine 49
Cysteine 70 of Prostasin and cysteine 49
Intramolecular
Cysteine 40 and cysteine 1055
3fp7 I 5 J 55
A redox-regulated disulphide may form between two units of Pancreatic trypsin inhibitor at cysteines 40 and 90 (5 and 55 respectively in this structure).
Details
Redox score ?
87
PDB code
3fp7
Structure name
anionic trypsin variant s195a in complex with bovine pancreatic trypsin inhibitor (bpti) cleaved at the scissile bond (lys15-ala16) determined to the 1
Structure deposition date
2009-01-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Pancreatic trypsin inhibitor
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
P00974
Peptide B accession
P00974
Peptide A residue number
40
Peptide B residue number
90
Ligandability
Cysteine 40 of Pancreatic trypsin inhibitor
Cysteine 90 of Pancreatic trypsin inhibitor
3gym A 58 I 14
A redox-regulated disulphide may form between cysteine 86 of Prostasin and cysteine 49 of Pancreatic trypsin inhibitor (58 and 14 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
3gym
Structure name
structure of prostasin in complex with aprotinin
Structure deposition date
2009-04-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prostasin
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q16651
Peptide B accession
P00974
Peptide A residue number
86
Peptide B residue number
49
Ligandability
Cysteine 86 of Prostasin
Cysteine 49 of Pancreatic trypsin inhibitor
2r9p B 58 F 14
A redox-regulated disulphide may form between cysteine 121 of Trypsin-3 and cysteine 49 of Pancreatic trypsin inhibitor (58 and 14 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
2r9p
Structure name
human mesotrypsin complexed with bovine pancreatic trypsin inhibitor(bpti)
Structure deposition date
2007-09-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide A name
Trypsin-3
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
P35030
Peptide B accession
P00974
Peptide A residue number
121
Peptide B residue number
49
Ligandability
Cysteine 121 of Trypsin-3
Cysteine 49 of Pancreatic trypsin inhibitor
1eaw C 58 D 14
A redox-regulated disulphide may form between cysteine 657 of Suppressor of tumorigenicity 14 protein and cysteine 49 of Pancreatic trypsin inhibitor (58 and 14 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
1eaw
Structure name
crystal structure of the mtsp1 (matriptase)-bpti (aprotinin) complex
Structure deposition date
2001-07-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
100
Minimum pKa ?
nan
% buried
nan
Peptide A name
Suppressor of tumorigenicity 14 protein
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q9Y5Y6
Peptide B accession
P00974
Peptide A residue number
657
Peptide B residue number
49
Ligandability
Cysteine 657 of Suppressor of tumorigenicity 14 protein
Cysteine 49 of Pancreatic trypsin inhibitor
2kai A 58 I 14
A redox-regulated disulphide may form between cysteine 49 of Glandular kallikrein and cysteine 49 of Pancreatic trypsin inhibitor (58 and 14 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
2kai
Structure name
refined 2
Structure deposition date
1984-05-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glandular kallikrein
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
P00752
Peptide B accession
P00974
Peptide A residue number
49
Peptide B residue number
49
Ligandability
Cysteine 49 of Glandular kallikrein
Cysteine 49 of Pancreatic trypsin inhibitor
3p92 A 58 E 14
A redox-regulated disulphide may form between cysteine 68 of PRSS3 protein and cysteine 49 of Pancreatic trypsin inhibitor (58 and 14 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
3p92
Structure name
human mesotrypsin complexed with bovine pancreatic trypsin inhibitor variant (bpti-k15r/r17g)
Structure deposition date
2010-10-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q8N2U3
Peptide B accession
P00974
Peptide A residue number
68
Peptide B residue number
49
Ligandability
Cysteine 68 of PRSS3 protein
Cysteine 49 of Pancreatic trypsin inhibitor
4bnr B 58 J 14
A redox-regulated disulphide may form between cysteine 46 of Hepatopancreas trypsin and cysteine 49 of Pancreatic trypsin inhibitor (58 and 14 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
4bnr
Structure name
extremely stable complex of crayfish trypsin with bovine trypsin inhibitor
Structure deposition date
2013-05-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepatopancreas trypsin
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q52V24
Peptide B accession
P00974
Peptide A residue number
46
Peptide B residue number
49
Ligandability
Cysteine 46 of Hepatopancreas trypsin
Cysteine 49 of Pancreatic trypsin inhibitor
1fak H 58 I 14
A redox-regulated disulphide may form between cysteine 254 of Coagulation factor VII and cysteine 49 of Pancreatic trypsin inhibitor (58 and 14 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
1fak
Structure name
human tissue factor complexed with coagulation factor viia inhibited with a bpti-mutant
Structure deposition date
1998-12-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor VII
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
P08709
Peptide B accession
P00974
Peptide A residue number
254
Peptide B residue number
49
Ligandability
Cysteine 254 of Coagulation factor VII
Cysteine 49 of Pancreatic trypsin inhibitor
2r9p A 42 E 14
A redox-regulated disulphide may form between cysteine 105 of Trypsin-3 and cysteine 49 of Pancreatic trypsin inhibitor (42 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
2r9p
Structure name
human mesotrypsin complexed with bovine pancreatic trypsin inhibitor(bpti)
Structure deposition date
2007-09-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide A name
Trypsin-3
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
P35030
Peptide B accession
P00974
Peptide A residue number
105
Peptide B residue number
49
Ligandability
Cysteine 105 of Trypsin-3
Cysteine 49 of Pancreatic trypsin inhibitor
4dg4 G 42 H 14
A redox-regulated disulphide may form between cysteine 52 of PRSS3 protein and cysteine 49 of Pancreatic trypsin inhibitor (42 and 14 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
4dg4
Structure name
human mesotrypsin-s39y complexed with bovine pancreatic trypsin inhibitor (bpti)
Structure deposition date
2012-01-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
PRSS3 protein
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q8N2U3
Peptide B accession
P00974
Peptide A residue number
52
Peptide B residue number
49
Ligandability
Cysteine 52 of PRSS3 protein
Cysteine 49 of Pancreatic trypsin inhibitor
1fak H 42 I 14
A redox-regulated disulphide may form between cysteine 238 of Coagulation factor VII and cysteine 49 of Pancreatic trypsin inhibitor (42 and 14 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
1fak
Structure name
human tissue factor complexed with coagulation factor viia inhibited with a bpti-mutant
Structure deposition date
1998-12-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
100
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor VII
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
P08709
Peptide B accession
P00974
Peptide A residue number
238
Peptide B residue number
49
Ligandability
Cysteine 238 of Coagulation factor VII
Cysteine 49 of Pancreatic trypsin inhibitor
1eaw A 42 B 14
A redox-regulated disulphide may form between cysteine 641 of Suppressor of tumorigenicity 14 protein and cysteine 49 of Pancreatic trypsin inhibitor (42 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
1eaw
Structure name
crystal structure of the mtsp1 (matriptase)-bpti (aprotinin) complex
Structure deposition date
2001-07-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide A name
Suppressor of tumorigenicity 14 protein
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q9Y5Y6
Peptide B accession
P00974
Peptide A residue number
641
Peptide B residue number
49
Ligandability
Cysteine 641 of Suppressor of tumorigenicity 14 protein
Cysteine 49 of Pancreatic trypsin inhibitor
4bnr B 42 J 14
A redox-regulated disulphide may form between cysteine 30 of Hepatopancreas trypsin and cysteine 49 of Pancreatic trypsin inhibitor (42 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
4bnr
Structure name
extremely stable complex of crayfish trypsin with bovine trypsin inhibitor
Structure deposition date
2013-05-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepatopancreas trypsin
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q52V24
Peptide B accession
P00974
Peptide A residue number
30
Peptide B residue number
49
Ligandability
Cysteine 30 of Hepatopancreas trypsin
Cysteine 49 of Pancreatic trypsin inhibitor
2kai A 42 I 14
A redox-regulated disulphide may form between cysteine 33 of Glandular kallikrein and cysteine 49 of Pancreatic trypsin inhibitor (42 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
2kai
Structure name
refined 2
Structure deposition date
1984-05-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glandular kallikrein
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
P00752
Peptide B accession
P00974
Peptide A residue number
33
Peptide B residue number
49
Ligandability
Cysteine 33 of Glandular kallikrein
Cysteine 49 of Pancreatic trypsin inhibitor
3gym A 42 I 14
A redox-regulated disulphide may form between cysteine 70 of Prostasin and cysteine 49 of Pancreatic trypsin inhibitor (42 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
3gym
Structure name
structure of prostasin in complex with aprotinin
Structure deposition date
2009-04-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prostasin
Peptide B name
Pancreatic trypsin inhibitor
Peptide A accession
Q16651
Peptide B accession
P00974
Peptide A residue number
70
Peptide B residue number
49
Ligandability
Cysteine 70 of Prostasin
Cysteine 49 of Pancreatic trypsin inhibitor
5jb4 A 1005 A 1055
A redox-regulated disulphide may form within Pancreatic trypsin inhibitor between cysteines 40 and 1055 (1005 and 1055 respectively in this structure).
Details
Redox score ?
nan
PDB code
5jb4
Structure name
a simplified bpti variant containing 21 alanines out 58 of residues
Structure deposition date
2016-04-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00974
Residue number A
40
Residue number B
1055
Peptide name
Pancreatic trypsin inhibitor
Ligandability
Cysteine 40 of Pancreatic trypsin inhibitor
Cysteine 1055 of Pancreatic trypsin inhibitor
Cysteine 1055 in protein B could not be asigned to a Uniprot residue.
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