Coagulation factor XII
Intramolecular
Cysteine 161 and cysteine 170
Cysteine 135 and cysteine 163
Cysteine 178 and cysteine 189
Cysteine 200 and cysteine 209
Cysteine 436 and cysteine 439
Cysteine 486 and cysteine 306
Cysteine 61 and cysteine 88
Cysteine 183 and cysteine 198
Cysteine 500 and cysteine 569
Cysteine 47 and cysteine 73
More...Cysteine 532 and cysteine 548
Cysteine 405 and cysteine 475
Cysteine 359 and cysteine 486
Cysteine 397 and cysteine 413
Cysteine 559 and cysteine 590
Cysteine 47 and cysteine 88
Cysteine 47 and cysteine 61
Cysteine 73 and cysteine 88
Cysteine 183 and cysteine 189
Cysteine 183 and cysteine 209
Cysteine 198 and cysteine 209
Cysteine 61 and cysteine 73
Cysteine 178 and cysteine 183
Cysteine 189 and cysteine 198
Cysteine 183 and cysteine 200
Cysteine 198 and cysteine 200
Cysteine 178 and cysteine 198
Cysteine 135 and cysteine 170
Cysteine 135 and cysteine 161
Cysteine 163 and cysteine 170
Cysteine 189 and cysteine 209
Cysteine 161 and cysteine 163
4bdw A 31 A 40
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 161 and 170 (31 and 40 respectively in this structure).
Details
Redox score ?
88
PDB code
4bdw
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii in complex with holmium
Structure deposition date
2012-10-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
161
Residue number B
170
Peptide name
Coagulation factor XII
Ligandability
Cysteine 161 of Coagulation factor XII
Cysteine 170 of Coagulation factor XII
4bdw A 5 A 33
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 135 and 163 (5 and 33 respectively in this structure).
Details
Redox score ?
87
PDB code
4bdw
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii in complex with holmium
Structure deposition date
2012-10-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
135
Residue number B
163
Peptide name
Coagulation factor XII
Ligandability
Cysteine 135 of Coagulation factor XII
Cysteine 163 of Coagulation factor XII
4bdw A 48 A 59
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 178 and 189 (48 and 59 respectively in this structure).
Details
Redox score ?
86
PDB code
4bdw
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii in complex with holmium
Structure deposition date
2012-10-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
178
Residue number B
189
Peptide name
Coagulation factor XII
Ligandability
Cysteine 178 of Coagulation factor XII
Cysteine 189 of Coagulation factor XII
4bdw A 70 A 79
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 200 and 209 (70 and 79 respectively in this structure).
Details
Redox score ?
86
PDB code
4bdw
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii in complex with holmium
Structure deposition date
2012-10-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
200
Residue number B
209
Peptide name
Coagulation factor XII
Ligandability
Cysteine 200 of Coagulation factor XII
Cysteine 209 of Coagulation factor XII
6qf7 D 417 D 420
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 436 and 439 (417 and 420 respectively in this structure).
Details
Redox score ?
86
PDB code
6qf7
Structure name
crystal structures of the recombinant beta-factor xiia protease with bound thr-arg and pro-arg substrate mimetics
Structure deposition date
2019-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
436
Residue number B
439
Peptide name
Coagulation factor XII
Ligandability
Cysteine 436 of Coagulation factor XII
Cysteine 439 of Coagulation factor XII
6gt6 B 122 B 306
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 486 and 306 (122 and 306 respectively in this structure).
Details
Redox score ?
85
PDB code
6gt6
Structure name
crystal structure of recombinant coagulation factor beta-xiia
Structure deposition date
2018-06-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
486
Residue number B
306
Peptide name
Coagulation factor XII
Ligandability
Cysteine 486 of Coagulation factor XII
Cysteine 306 of Coagulation factor XII
Cysteine 306 in protein B could not be asigned to a Uniprot residue.
7prj A 42 A 69
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 61 and 88 (42 and 69 respectively in this structure).
Details
Redox score ?
85
PDB code
7prj
Structure name
factor xii fibronectin type ii (fxii fnii) domain
Structure deposition date
2021-09-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
61
Residue number B
88
Peptide name
Coagulation factor XII
Ligandability
Cysteine 61 of Coagulation factor XII
Cysteine 88 of Coagulation factor XII
4bdw A 53 A 68
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 183 and 198 (53 and 68 respectively in this structure).
Details
Redox score ?
85
PDB code
4bdw
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii in complex with holmium
Structure deposition date
2012-10-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
183
Residue number B
198
Peptide name
Coagulation factor XII
Ligandability
Cysteine 183 of Coagulation factor XII
Cysteine 198 of Coagulation factor XII
6b74 B 136 B 201
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 500 and 569 (136 and 201 respectively in this structure).
Details
Redox score ?
84
PDB code
6b74
Structure name
structures of the two-chain human plasma factor xiia co-crystallized with potent inhibitors
Structure deposition date
2017-10-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
500
Residue number B
569
Peptide name
Coagulation factor XII
Ligandability
Cysteine 500 of Coagulation factor XII
Cysteine 569 of Coagulation factor XII
6szw D 28 D 54
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 47 and 73 (28 and 54 respectively in this structure).
Details
Redox score ?
83
PDB code
6szw
Structure name
asymmetric complex of factor xii and kininogen with gc1qr/c1qbp/p32 is governed by allostery
Structure deposition date
2019-10-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
47
Residue number B
73
Peptide name
Coagulation factor XII
Ligandability
Cysteine 47 of Coagulation factor XII
Cysteine 73 of Coagulation factor XII
7fbp A 532 A 548
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 532 and 548.
Details
Redox score ?
83
PDB code
7fbp
Structure name
fxiia-cmcofx1 complex
Structure deposition date
2021-07-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
532
Residue number B
548
Peptide name
Coagulation factor XII
Ligandability
Cysteine 532 of Coagulation factor XII
Cysteine 548 of Coagulation factor XII
6b74 B 50 B 111
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 405 and 475 (50 and 111 respectively in this structure).
Details
Redox score ?
82
PDB code
6b74
Structure name
structures of the two-chain human plasma factor xiia co-crystallized with potent inhibitors
Structure deposition date
2017-10-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
405
Residue number B
475
Peptide name
Coagulation factor XII
Ligandability
Cysteine 405 of Coagulation factor XII
Cysteine 475 of Coagulation factor XII
6x0t C 359 C 486
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 359 and 486.
Details
Redox score ?
80
PDB code
6x0t
Structure name
structure of human plasma factor xiia in complex with (2s)-1-(n,3- dicyclohexyl-d-alanyl)-4-[(4r,5s)-4-methyl-5-phenyl-4,5-dihydro-1,3- oxazol-2-yl]-n-[(thiophen-2-yl)methyl]piperazine-2-carboxamide (compound 8h)
Structure deposition date
2020-05-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
359
Residue number B
486
Peptide name
Coagulation factor XII
Ligandability
Cysteine 359 of Coagulation factor XII
Cysteine 486 of Coagulation factor XII
6x0t A 397 A 413
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 397 and 413.
Details
Redox score ?
80
PDB code
6x0t
Structure name
structure of human plasma factor xiia in complex with (2s)-1-(n,3- dicyclohexyl-d-alanyl)-4-[(4r,5s)-4-methyl-5-phenyl-4,5-dihydro-1,3- oxazol-2-yl]-n-[(thiophen-2-yl)methyl]piperazine-2-carboxamide (compound 8h)
Structure deposition date
2020-05-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
397
Residue number B
413
Peptide name
Coagulation factor XII
Ligandability
Cysteine 397 of Coagulation factor XII
Cysteine 413 of Coagulation factor XII
6gt6 B 191 B 220
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 559 and 590 (191 and 220 respectively in this structure).
Details
Redox score ?
80
PDB code
6gt6
Structure name
crystal structure of recombinant coagulation factor beta-xiia
Structure deposition date
2018-06-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
559
Residue number B
590
Peptide name
Coagulation factor XII
Ligandability
Cysteine 559 of Coagulation factor XII
Cysteine 590 of Coagulation factor XII
7prk A 28 A 69
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 47 and 88 (28 and 69 respectively in this structure).
Details
Redox score ?
76
PDB code
7prk
Structure name
factor xii fibronectin type ii (fxii fnii) domain
Structure deposition date
2021-09-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
47
Residue number B
88
Peptide name
Coagulation factor XII
Ligandability
Cysteine 47 of Coagulation factor XII
Cysteine 88 of Coagulation factor XII
7prk A 28 A 42
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 47 and 61 (28 and 42 respectively in this structure).
Details
Redox score ?
73
PDB code
7prk
Structure name
factor xii fibronectin type ii (fxii fnii) domain
Structure deposition date
2021-09-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
47
Residue number B
61
Peptide name
Coagulation factor XII
Ligandability
Cysteine 47 of Coagulation factor XII
Cysteine 61 of Coagulation factor XII
7prk A 54 A 69
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 73 and 88 (54 and 69 respectively in this structure).
Details
Redox score ?
72
PDB code
7prk
Structure name
factor xii fibronectin type ii (fxii fnii) domain
Structure deposition date
2021-09-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
73
Residue number B
88
Peptide name
Coagulation factor XII
Ligandability
Cysteine 73 of Coagulation factor XII
Cysteine 88 of Coagulation factor XII
4bdw A 53 A 59
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 183 and 189 (53 and 59 respectively in this structure).
Details
Redox score ?
71
PDB code
4bdw
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii in complex with holmium
Structure deposition date
2012-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
183
Residue number B
189
Peptide name
Coagulation factor XII
Ligandability
Cysteine 183 of Coagulation factor XII
Cysteine 189 of Coagulation factor XII
4bdw A 53 A 79
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 183 and 209 (53 and 79 respectively in this structure).
Details
Redox score ?
71
PDB code
4bdw
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii in complex with holmium
Structure deposition date
2012-10-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
183
Residue number B
209
Peptide name
Coagulation factor XII
Ligandability
Cysteine 183 of Coagulation factor XII
Cysteine 209 of Coagulation factor XII
4bdx A 68 A 79
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 198 and 209 (68 and 79 respectively in this structure).
Details
Redox score ?
68
PDB code
4bdx
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii
Structure deposition date
2012-10-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
198
Residue number B
209
Peptide name
Coagulation factor XII
Ligandability
Cysteine 198 of Coagulation factor XII
Cysteine 209 of Coagulation factor XII
7prj A 42 A 54
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 61 and 73 (42 and 54 respectively in this structure).
Details
Redox score ?
68
PDB code
7prj
Structure name
factor xii fibronectin type ii (fxii fnii) domain
Structure deposition date
2021-09-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
61
Residue number B
73
Peptide name
Coagulation factor XII
Ligandability
Cysteine 61 of Coagulation factor XII
Cysteine 73 of Coagulation factor XII
4bdx A 48 A 53
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 178 and 183 (48 and 53 respectively in this structure).
Details
Redox score ?
66
PDB code
4bdx
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii
Structure deposition date
2012-10-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
178
Residue number B
183
Peptide name
Coagulation factor XII
Ligandability
Cysteine 178 of Coagulation factor XII
Cysteine 183 of Coagulation factor XII
4bdx A 59 A 68
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 189 and 198 (59 and 68 respectively in this structure).
Details
Redox score ?
63
PDB code
4bdx
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii
Structure deposition date
2012-10-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
189
Residue number B
198
Peptide name
Coagulation factor XII
Ligandability
Cysteine 189 of Coagulation factor XII
Cysteine 198 of Coagulation factor XII
4bdx A 53 A 70
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 183 and 200 (53 and 70 respectively in this structure).
Details
Redox score ?
62
PDB code
4bdx
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii
Structure deposition date
2012-10-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
183
Residue number B
200
Peptide name
Coagulation factor XII
Ligandability
Cysteine 183 of Coagulation factor XII
Cysteine 200 of Coagulation factor XII
4bdw A 68 A 70
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 198 and 200 (68 and 70 respectively in this structure).
Details
Redox score ?
60
PDB code
4bdw
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii in complex with holmium
Structure deposition date
2012-10-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
198
Residue number B
200
Peptide name
Coagulation factor XII
Ligandability
Cysteine 198 of Coagulation factor XII
Cysteine 200 of Coagulation factor XII
4bdx A 48 A 68
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 178 and 198 (48 and 68 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
4bdx
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii
Structure deposition date
2012-10-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
178
Residue number B
198
Peptide name
Coagulation factor XII
Ligandability
Cysteine 178 of Coagulation factor XII
Cysteine 198 of Coagulation factor XII
4bdx A 5 A 40
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 135 and 170 (5 and 40 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
4bdx
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii
Structure deposition date
2012-10-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
135
Residue number B
170
Peptide name
Coagulation factor XII
Ligandability
Cysteine 135 of Coagulation factor XII
Cysteine 170 of Coagulation factor XII
4bdx A 5 A 31
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 135 and 161 (5 and 31 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4bdx
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii
Structure deposition date
2012-10-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
135
Residue number B
161
Peptide name
Coagulation factor XII
Ligandability
Cysteine 135 of Coagulation factor XII
Cysteine 161 of Coagulation factor XII
4bdx A 33 A 40
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 163 and 170 (33 and 40 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
4bdx
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii
Structure deposition date
2012-10-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
163
Residue number B
170
Peptide name
Coagulation factor XII
Ligandability
Cysteine 163 of Coagulation factor XII
Cysteine 170 of Coagulation factor XII
4bdw A 59 A 79
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 189 and 209 (59 and 79 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
4bdw
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii in complex with holmium
Structure deposition date
2012-10-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
189
Residue number B
209
Peptide name
Coagulation factor XII
Ligandability
Cysteine 189 of Coagulation factor XII
Cysteine 209 of Coagulation factor XII
4bdx A 31 A 33
A redox-regulated disulphide may form within Coagulation factor XII between cysteines 161 and 163 (31 and 33 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
4bdx
Structure name
the structure of the fni-egf tandem domain of coagulation factor xii
Structure deposition date
2012-10-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00748
Residue number A
161
Residue number B
163
Peptide name
Coagulation factor XII
Ligandability
Cysteine 161 of Coagulation factor XII
Cysteine 163 of Coagulation factor XII
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