Plasma kallikrein
Intramolecular
Cysteine 340 and cysteine 345
Cysteine 201 and cysteine 284
Cysteine 21 and cysteine 104
Cysteine 292 and cysteine 375
Cysteine 517 and cysteine 584
Cysteine 111 and cysteine 194
Cysteine 51 and cysteine 57
Cysteine 318 and cysteine 347
Cysteine 383 and cysteine 503
Cysteine 141 and cysteine 147
More...Cysteine 231 and cysteine 237
Cysteine 548 and cysteine 563
Cysteine 227 and cysteine 256
Cysteine 137 and cysteine 166
Cysteine 322 and cysteine 328
Cysteine 231 and cysteine 503
Cysteine 47 and cysteine 77
Cysteine 419 and cysteine 435
Cysteine 574 and cysteine 602
Cysteine 21 and cysteine 231
Cysteine 21 and cysteine 383
Cysteine 227 and cysteine 231
Cysteine 318 and cysteine 322
Cysteine 47 and cysteine 51
Cysteine 227 and cysteine 237
Cysteine 237 and cysteine 256
Cysteine 47 and cysteine 57
Cysteine 322 and cysteine 347
Cysteine 137 and cysteine 141
Cysteine 137 and cysteine 147
Cysteine 328 and cysteine 347
Cysteine 147 and cysteine 166
Cysteine 231 and cysteine 256
Cysteine 141 and cysteine 166
Cysteine 318 and cysteine 328
Cysteine 104 and cysteine 231
Cysteine 57 and cysteine 77
Cysteine 104 and cysteine 383
Cysteine 21 and cysteine 503
Cysteine 51 and cysteine 77
6o1g A 340 A 345
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 340 and 345.
Details
Redox score ?
87
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
340
Residue number B
345
Peptide name
Plasma kallikrein
Ligandability
Cysteine 340 of Plasma kallikrein
Cysteine 345 of Plasma kallikrein
7qox B 182 B 265
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 201 and 284 (182 and 265 respectively in this structure).
Details
Redox score ?
87
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
201
Residue number B
284
Peptide name
Plasma kallikrein
Ligandability
Cysteine 201 of Plasma kallikrein
Cysteine 284 of Plasma kallikrein
7qox B 2 B 85
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 21 and 104 (2 and 85 respectively in this structure).
Details
Redox score ?
85
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
21
Residue number B
104
Peptide name
Plasma kallikrein
Ligandability
Cysteine 21 of Plasma kallikrein
Cysteine 104 of Plasma kallikrein
7qox B 273 B 356
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 292 and 375 (273 and 356 respectively in this structure).
Details
Redox score ?
84
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
292
Residue number B
375
Peptide name
Plasma kallikrein
Ligandability
Cysteine 292 of Plasma kallikrein
Cysteine 375 of Plasma kallikrein
2any A 136 A 201
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 517 and 584 (136 and 201 respectively in this structure).
Details
Redox score ?
83
PDB code
2any
Structure name
expression, crystallization and the three-dimensional structure of the catalytic domain of human plasma kallikrein: implications for structure-based design of protease inhibitors
Structure deposition date
2005-08-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
517
Residue number B
584
Peptide name
Plasma kallikrein
Ligandability
Cysteine 517 of Plasma kallikrein
Cysteine 584 of Plasma kallikrein
7qox A 92 A 175
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 111 and 194 (92 and 175 respectively in this structure).
Details
Redox score ?
83
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
111
Residue number B
194
Peptide name
Plasma kallikrein
Ligandability
Cysteine 111 of Plasma kallikrein
Cysteine 194 of Plasma kallikrein
7qox B 32 B 38
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 51 and 57 (32 and 38 respectively in this structure).
Details
Redox score ?
82
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
51
Residue number B
57
Peptide name
Plasma kallikrein
Ligandability
Cysteine 51 of Plasma kallikrein
Cysteine 57 of Plasma kallikrein
6i44 A 299 A 328
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 318 and 347 (299 and 328 respectively in this structure).
Details
Redox score ?
82
PDB code
6i44
Structure name
allosteric activation of human prekallikrein by apple domain disc rotation
Structure deposition date
2018-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
318
Residue number B
347
Peptide name
Plasma kallikrein
Ligandability
Cysteine 318 of Plasma kallikrein
Cysteine 347 of Plasma kallikrein
6o1g A 383 A 503
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 383 and 503.
Details
Redox score ?
82
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
383
Residue number B
503
Peptide name
Plasma kallikrein
Ligandability
Cysteine 383 of Plasma kallikrein
Cysteine 503 of Plasma kallikrein
Cysteine 383 in protein A could not be asigned to a Uniprot residue.
7qox A 122 A 128
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 141 and 147 (122 and 128 respectively in this structure).
Details
Redox score ?
81
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
141
Residue number B
147
Peptide name
Plasma kallikrein
Ligandability
Cysteine 141 of Plasma kallikrein
Cysteine 147 of Plasma kallikrein
7qox A 212 A 218
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 231 and 237 (212 and 218 respectively in this structure).
Details
Redox score ?
81
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
231
Residue number B
237
Peptide name
Plasma kallikrein
Ligandability
Cysteine 231 of Plasma kallikrein
Cysteine 237 of Plasma kallikrein
5tjx A 548 A 563
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 548 and 563.
Details
Redox score ?
81
PDB code
5tjx
Structure name
structure of human plasma kallikrein
Structure deposition date
2016-10-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
548
Residue number B
563
Peptide name
Plasma kallikrein
Ligandability
Cysteine 548 of Plasma kallikrein
Cysteine 563 of Plasma kallikrein
7qox A 208 A 237
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 227 and 256 (208 and 237 respectively in this structure).
Details
Redox score ?
81
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
227
Residue number B
256
Peptide name
Plasma kallikrein
Ligandability
Cysteine 227 of Plasma kallikrein
Cysteine 256 of Plasma kallikrein
7qox A 118 A 147
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 137 and 166 (118 and 147 respectively in this structure).
Details
Redox score ?
81
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
137
Residue number B
166
Peptide name
Plasma kallikrein
Ligandability
Cysteine 137 of Plasma kallikrein
Cysteine 166 of Plasma kallikrein
7qox A 303 A 309
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 322 and 328 (303 and 309 respectively in this structure).
Details
Redox score ?
81
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
322
Residue number B
328
Peptide name
Plasma kallikrein
Ligandability
Cysteine 322 of Plasma kallikrein
Cysteine 328 of Plasma kallikrein
6i44 A 364 A 484
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 231 and 503 (364 and 484 respectively in this structure).
Details
Redox score ?
81
PDB code
6i44
Structure name
allosteric activation of human prekallikrein by apple domain disc rotation
Structure deposition date
2018-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
231
Residue number B
503
Peptide name
Plasma kallikrein
Ligandability
Cysteine 231 of Plasma kallikrein
Cysteine 503 of Plasma kallikrein
6o1g A 47 A 77
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 47 and 77.
Details
Redox score ?
80
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
47
Residue number B
77
Peptide name
Plasma kallikrein
Ligandability
Cysteine 47 of Plasma kallikrein
Cysteine 77 of Plasma kallikrein
2anw A 42 A 58
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 419 and 435 (42 and 58 respectively in this structure).
Details
Redox score ?
80
PDB code
2anw
Structure name
expression, crystallization and three-dimensional structure of the catalytic domain of human plasma kallikrein: implications for structure-based design of protease inhibitors
Structure deposition date
2005-08-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
419
Residue number B
435
Peptide name
Plasma kallikrein
Ligandability
Cysteine 419 of Plasma kallikrein
Cysteine 435 of Plasma kallikrein
8a3q A 191 A 220
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 574 and 602 (191 and 220 respectively in this structure).
Details
Redox score ?
79
PDB code
8a3q
Structure name
human plasma kallekrein in complex with 14w
Structure deposition date
2022-06-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
574
Residue number B
602
Peptide name
Plasma kallikrein
Ligandability
Cysteine 574 of Plasma kallikrein
Cysteine 602 of Plasma kallikrein
6i44 A 2 A 364
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 21 and 231 (2 and 364 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
6i44
Structure name
allosteric activation of human prekallikrein by apple domain disc rotation
Structure deposition date
2018-11-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
21
Residue number B
231
Peptide name
Plasma kallikrein
Ligandability
Cysteine 21 of Plasma kallikrein
Cysteine 231 of Plasma kallikrein
6o1g A 21 A 383
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 21 and 383. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
21
Residue number B
383
Peptide name
Plasma kallikrein
Ligandability
Cysteine 21 of Plasma kallikrein
Cysteine 383 of Plasma kallikrein
Cysteine 383 in protein B could not be asigned to a Uniprot residue.
6i44 A 208 A 212
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 227 and 231 (208 and 212 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
6i44
Structure name
allosteric activation of human prekallikrein by apple domain disc rotation
Structure deposition date
2018-11-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
227
Residue number B
231
Peptide name
Plasma kallikrein
Ligandability
Cysteine 227 of Plasma kallikrein
Cysteine 231 of Plasma kallikrein
6o1g A 318 A 322
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 318 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
318
Residue number B
322
Peptide name
Plasma kallikrein
Ligandability
Cysteine 318 of Plasma kallikrein
Cysteine 322 of Plasma kallikrein
6o1g A 47 A 51
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 47 and 51. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
47
Residue number B
51
Peptide name
Plasma kallikrein
Ligandability
Cysteine 47 of Plasma kallikrein
Cysteine 51 of Plasma kallikrein
7qox A 208 A 218
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 227 and 237 (208 and 218 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
227
Residue number B
237
Peptide name
Plasma kallikrein
Ligandability
Cysteine 227 of Plasma kallikrein
Cysteine 237 of Plasma kallikrein
7qox B 218 B 237
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 237 and 256 (218 and 237 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
237
Residue number B
256
Peptide name
Plasma kallikrein
Ligandability
Cysteine 237 of Plasma kallikrein
Cysteine 256 of Plasma kallikrein
6o1g A 47 A 57
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 47 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
47
Residue number B
57
Peptide name
Plasma kallikrein
Ligandability
Cysteine 47 of Plasma kallikrein
Cysteine 57 of Plasma kallikrein
6i44 A 303 A 328
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 322 and 347 (303 and 328 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6i44
Structure name
allosteric activation of human prekallikrein by apple domain disc rotation
Structure deposition date
2018-11-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
322
Residue number B
347
Peptide name
Plasma kallikrein
Ligandability
Cysteine 322 of Plasma kallikrein
Cysteine 347 of Plasma kallikrein
7qox B 118 B 122
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 137 and 141 (118 and 122 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
137
Residue number B
141
Peptide name
Plasma kallikrein
Ligandability
Cysteine 137 of Plasma kallikrein
Cysteine 141 of Plasma kallikrein
6i44 A 118 A 128
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 137 and 147 (118 and 128 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6i44
Structure name
allosteric activation of human prekallikrein by apple domain disc rotation
Structure deposition date
2018-11-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
137
Residue number B
147
Peptide name
Plasma kallikrein
Ligandability
Cysteine 137 of Plasma kallikrein
Cysteine 147 of Plasma kallikrein
7qox A 309 A 328
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 328 and 347 (309 and 328 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
328
Residue number B
347
Peptide name
Plasma kallikrein
Ligandability
Cysteine 328 of Plasma kallikrein
Cysteine 347 of Plasma kallikrein
6o1g A 147 A 166
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 147 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
147
Residue number B
166
Peptide name
Plasma kallikrein
Ligandability
Cysteine 147 of Plasma kallikrein
Cysteine 166 of Plasma kallikrein
6i44 A 212 A 237
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 231 and 256 (212 and 237 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6i44
Structure name
allosteric activation of human prekallikrein by apple domain disc rotation
Structure deposition date
2018-11-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
231
Residue number B
256
Peptide name
Plasma kallikrein
Ligandability
Cysteine 231 of Plasma kallikrein
Cysteine 256 of Plasma kallikrein
6o1g A 141 A 166
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 141 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
141
Residue number B
166
Peptide name
Plasma kallikrein
Ligandability
Cysteine 141 of Plasma kallikrein
Cysteine 166 of Plasma kallikrein
7qox A 299 A 309
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 318 and 328 (299 and 309 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
7qox
Structure name
factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes
Structure deposition date
2021-12-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
318
Residue number B
328
Peptide name
Plasma kallikrein
Ligandability
Cysteine 318 of Plasma kallikrein
Cysteine 328 of Plasma kallikrein
6i44 A 85 A 364
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 104 and 231 (85 and 364 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
6i44
Structure name
allosteric activation of human prekallikrein by apple domain disc rotation
Structure deposition date
2018-11-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
104
Residue number B
231
Peptide name
Plasma kallikrein
Ligandability
Cysteine 104 of Plasma kallikrein
Cysteine 231 of Plasma kallikrein
6o1g A 57 A 77
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 57 and 77. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
57
Residue number B
77
Peptide name
Plasma kallikrein
Ligandability
Cysteine 57 of Plasma kallikrein
Cysteine 77 of Plasma kallikrein
6o1g A 104 A 383
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 104 and 383. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
104
Residue number B
383
Peptide name
Plasma kallikrein
Ligandability
Cysteine 104 of Plasma kallikrein
Cysteine 383 of Plasma kallikrein
Cysteine 383 in protein B could not be asigned to a Uniprot residue.
6i44 A 2 A 484
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 21 and 503 (2 and 484 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
6i44
Structure name
allosteric activation of human prekallikrein by apple domain disc rotation
Structure deposition date
2018-11-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
21
Residue number B
503
Peptide name
Plasma kallikrein
Ligandability
Cysteine 21 of Plasma kallikrein
Cysteine 503 of Plasma kallikrein
6o1g A 51 A 77
A redox-regulated disulphide may form within Plasma kallikrein between cysteines 51 and 77. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6o1g
Structure name
full length human plasma kallikrein with inhibitor
Structure deposition date
2019-02-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P03952
Residue number A
51
Residue number B
77
Peptide name
Plasma kallikrein
Ligandability
Cysteine 51 of Plasma kallikrein
Cysteine 77 of Plasma kallikrein
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