Coagulation factor VII
Intermolecular
Cysteine 195 and cysteine 322
Cysteine 77 and cysteine 241 of Tissue factor
Cysteine 254 and cysteine 49 of Pancreatic trypsin inhibitor
Cysteine 187 and cysteine 322
Cysteine 238 and cysteine 49 of Pancreatic trypsin inhibitor
Intramolecular
Cysteine 77 and cysteine 82
Cysteine 110 and cysteine 121
Cysteine 158 and cysteine 172
Cysteine 174 and cysteine 187
Cysteine 132 and cysteine 141
More...Cysteine 115 and cysteine 130
Cysteine 151 and cysteine 162
Cysteine 219 and cysteine 224
Cysteine 370 and cysteine 389
Cysteine 238 and cysteine 254
Cysteine 115 and cysteine 121
Cysteine 400 and cysteine 428
Cysteine 158 and cysteine 162
Cysteine 130 and cysteine 141
Cysteine 151 and cysteine 158
Cysteine 121 and cysteine 130
Cysteine 162 and cysteine 172
Cysteine 130 and cysteine 132
Cysteine 110 and cysteine 115
Cysteine 115 and cysteine 141
Cysteine 151 and cysteine 172
Cysteine 115 and cysteine 132
Cysteine 172 and cysteine 187
Cysteine 91 and cysteine 111
Cysteine 158 and cysteine 187
Cysteine 121 and cysteine 132
Cysteine 172 and cysteine 174
Cysteine 121 and cysteine 141
Cysteine 158 and cysteine 174
Cysteine 110 and cysteine 132
Cysteine 110 and cysteine 141
Cysteine 187 and cysteine 195
Cysteine 238 and cysteine 428
1kli L 135 H 122
A redox-regulated disulphide may form between two units of Coagulation factor VII at cysteines 195 and 322 (135 and 122 respectively in this structure).
Details
Redox score ?
78
PDB code
1kli
Structure name
cofactor-and substrate-assisted activation of factor viia
Structure deposition date
2001-12-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor VII
Peptide B name
Coagulation factor VII
Peptide A accession
P08709
Peptide B accession
P08709
Peptide A residue number
195
Peptide B residue number
322
Ligandability
Cysteine 195 of Coagulation factor VII
Cysteine 322 of Coagulation factor VII
2aei L 17 T 209
A redox-regulated disulphide may form between cysteine 77 of Coagulation factor VII and cysteine 241 of Tissue factor (17 and 209 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
2aei
Structure name
crystal structure of a ternary complex of factor viia/tissue factor and 2-[[6-[3-(aminoiminomethyl)phenoxy]-3,5-difluro-4-[(1-methyl-3- phenylpropyl)amino]-2-pyridinyl]oxy]-benzoic acid
Structure deposition date
2005-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor VII
Peptide B name
Tissue factor
Peptide A accession
P08709
Peptide B accession
P13726
Peptide A residue number
77
Peptide B residue number
241
Ligandability
Cysteine 77 of Coagulation factor VII
Cysteine 241 of Tissue factor
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
1klj L 127 H 122
A redox-regulated disulphide may form between two units of Coagulation factor VII at cysteines 187 and 322 (127 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 ?
39
PDB code
1klj
Structure name
crystal structure of uninhibited factor viia
Structure deposition date
2001-12-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor VII
Peptide B name
Coagulation factor VII
Peptide A accession
P08709
Peptide B accession
P08709
Peptide A residue number
187
Peptide B residue number
322
Ligandability
Cysteine 187 of Coagulation factor VII
Cysteine 322 of Coagulation factor VII
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
2b8o L 17 L 22
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 77 and 82 (17 and 22 respectively in this structure).
Details
Redox score ?
92
PDB code
2b8o
Structure name
crystal structure of glu-gly-arg-chloromethyl ketone-factor viia/soluble tissue factor complex
Structure deposition date
2005-10-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
77
Residue number B
82
Peptide name
Coagulation factor VII
Ligandability
Cysteine 77 of Coagulation factor VII
Cysteine 82 of Coagulation factor VII
2aei L 50 L 61
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 110 and 121 (50 and 61 respectively in this structure).
Details
Redox score ?
88
PDB code
2aei
Structure name
crystal structure of a ternary complex of factor viia/tissue factor and 2-[[6-[3-(aminoiminomethyl)phenoxy]-3,5-difluro-4-[(1-methyl-3- phenylpropyl)amino]-2-pyridinyl]oxy]-benzoic acid
Structure deposition date
2005-07-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
110
Residue number B
121
Peptide name
Coagulation factor VII
Ligandability
Cysteine 110 of Coagulation factor VII
Cysteine 121 of Coagulation factor VII
5l30 L 98 L 112
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 158 and 172 (98 and 112 respectively in this structure).
Details
Redox score ?
87
PDB code
5l30
Structure name
factor viia in complex with the inhibitor (2r,15r)-2-[(1- aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-7-[1-(1h-tetrazol-5- yl)cyclopropyl]-13-oxa-4,11-diazatricyclo[14
Structure deposition date
2016-08-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
158
Residue number B
172
Peptide name
Coagulation factor VII
Ligandability
Cysteine 158 of Coagulation factor VII
Cysteine 172 of Coagulation factor VII
1o5d L 114 L 127
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 174 and 187 (114 and 127 respectively in this structure).
Details
Redox score ?
87
PDB code
1o5d
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 ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
174
Residue number B
187
Peptide name
Coagulation factor VII
Ligandability
Cysteine 174 of Coagulation factor VII
Cysteine 187 of Coagulation factor VII
2b7d L 72 L 81
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 132 and 141 (72 and 81 respectively in this structure).
Details
Redox score ?
86
PDB code
2b7d
Structure name
factor viia inhibitors: chemical optimization, preclinical pharmacokinetics, pharmacodynamics, and efficacy in a baboon thrombosis model
Structure deposition date
2005-10-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
132
Residue number B
141
Peptide name
Coagulation factor VII
Ligandability
Cysteine 132 of Coagulation factor VII
Cysteine 141 of Coagulation factor VII
1wtg L 55 L 70
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 115 and 130 (55 and 70 respectively in this structure).
Details
Redox score ?
85
PDB code
1wtg
Structure name
human factor viia-tissue factor complexed with ethylsulfonamide-d- biphenylalanine-gln-p-aminobenzamidine
Structure deposition date
2004-11-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
115
Residue number B
130
Peptide name
Coagulation factor VII
Ligandability
Cysteine 115 of Coagulation factor VII
Cysteine 130 of Coagulation factor VII
2ec9 L 91 L 102
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 151 and 162 (91 and 102 respectively in this structure).
Details
Redox score ?
85
PDB code
2ec9
Structure name
crystal structure analysis of human factor viia , souluble tissue factor complexed with bcx-3607
Structure deposition date
2007-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
151
Residue number B
162
Peptide name
Coagulation factor VII
Ligandability
Cysteine 151 of Coagulation factor VII
Cysteine 162 of Coagulation factor VII
2c4f H 22 H 27
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 219 and 224 (22 and 27 respectively in this structure).
Details
Redox score ?
83
PDB code
2c4f
Structure name
crystal structure of factor vii
Structure deposition date
2005-10-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
219
Residue number B
224
Peptide name
Coagulation factor VII
Ligandability
Cysteine 219 of Coagulation factor VII
Cysteine 224 of Coagulation factor VII
2aer H 168 H 182
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 370 and 389 (168 and 182 respectively in this structure).
Details
Redox score ?
82
PDB code
2aer
Structure name
crystal structure of benzamidine-factor viia/soluble tissue factor complex
Structure deposition date
2005-07-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
370
Residue number B
389
Peptide name
Coagulation factor VII
Ligandability
Cysteine 370 of Coagulation factor VII
Cysteine 389 of Coagulation factor VII
2b8o H 42 H 58
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 238 and 254 (42 and 58 respectively in this structure).
Details
Redox score ?
81
PDB code
2b8o
Structure name
crystal structure of glu-gly-arg-chloromethyl ketone-factor viia/soluble tissue factor complex
Structure deposition date
2005-10-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
238
Residue number B
254
Peptide name
Coagulation factor VII
Ligandability
Cysteine 238 of Coagulation factor VII
Cysteine 254 of Coagulation factor VII
1j9c L 55 L 61
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 115 and 121 (55 and 61 respectively in this structure).
Details
Redox score ?
80
PDB code
1j9c
Structure name
crystal structure of tissue factor-factor viia complex
Structure deposition date
2001-05-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
115
Residue number B
121
Peptide name
Coagulation factor VII
Ligandability
Cysteine 115 of Coagulation factor VII
Cysteine 121 of Coagulation factor VII
4na9 H 191 H 220
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 400 and 428 (191 and 220 respectively in this structure).
Details
Redox score ?
79
PDB code
4na9
Structure name
factor viia in complex with the inhibitor 3'-amino-5'-[(2s,4r)-6- carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]biphenyl-2- carboxylic acid
Structure deposition date
2013-10-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
400
Residue number B
428
Peptide name
Coagulation factor VII
Ligandability
Cysteine 400 of Coagulation factor VII
Cysteine 428 of Coagulation factor VII
1jbu L 98 L 102
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 158 and 162 (98 and 102 respectively in this structure).
Details
Redox score ?
76
PDB code
1jbu
Structure name
coagulation factor vii zymogen (egf2/protease) in complex with inhibitory exosite peptide a-183
Structure deposition date
2001-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
158
Residue number B
162
Peptide name
Coagulation factor VII
Ligandability
Cysteine 158 of Coagulation factor VII
Cysteine 162 of Coagulation factor VII
5l0s B 70 B 81
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 130 and 141 (70 and 81 respectively in this structure).
Details
Redox score ?
70
PDB code
5l0s
Structure name
human poglut1 in complex with factor vii egf1 and udp
Structure deposition date
2016-07-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
130
Residue number B
141
Peptide name
Coagulation factor VII
Ligandability
Cysteine 130 of Coagulation factor VII
Cysteine 141 of Coagulation factor VII
1w8b L 91 L 98
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 151 and 158 (91 and 98 respectively in this structure).
Details
Redox score ?
67
PDB code
1w8b
Structure name
factor7 - 413 complex
Structure deposition date
2004-09-17
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
151
Residue number B
158
Peptide name
Coagulation factor VII
Ligandability
Cysteine 151 of Coagulation factor VII
Cysteine 158 of Coagulation factor VII
2a2q L 61 L 70
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 121 and 130 (61 and 70 respectively in this structure).
Details
Redox score ?
67
PDB code
2a2q
Structure name
complex of active-site inhibited human coagulation factor viia with human soluble tissue factor in the presence of ca2+, mg2+, na+, and zn2+
Structure deposition date
2005-06-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
121
Residue number B
130
Peptide name
Coagulation factor VII
Ligandability
Cysteine 121 of Coagulation factor VII
Cysteine 130 of Coagulation factor VII
4ng9 L 102 L 112
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 162 and 172 (102 and 112 respectively in this structure).
Details
Redox score ?
66
PDB code
4ng9
Structure name
factor viia in complex with the inhibitor (2r)-2-[(1-aminoisoquinolin- 6-yl)amino]-2-[3-ethoxy-4-(propan-2-yloxy)phenyl]-n-(3- sulfamoylbenzyl)ethanamide
Structure deposition date
2013-11-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
162
Residue number B
172
Peptide name
Coagulation factor VII
Ligandability
Cysteine 162 of Coagulation factor VII
Cysteine 172 of Coagulation factor VII
1qfk L 70 L 72
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 130 and 132 (70 and 72 respectively in this structure).
Details
Redox score ?
66
PDB code
1qfk
Structure name
structure of human factor viia and its implications for the triggering of blood coagulation
Structure deposition date
1999-04-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
130
Residue number B
132
Peptide name
Coagulation factor VII
Ligandability
Cysteine 130 of Coagulation factor VII
Cysteine 132 of Coagulation factor VII
3th3 L 50 L 55
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 110 and 115 (50 and 55 respectively in this structure).
Details
Redox score ?
64
PDB code
3th3
Structure name
mg2+ is required for optimal folding of the gamma-carboxyglutamic acid (gla) domains of vitamin k-dependent clotting factors at physiological ca2+
Structure deposition date
2011-08-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
110
Residue number B
115
Peptide name
Coagulation factor VII
Ligandability
Cysteine 110 of Coagulation factor VII
Cysteine 115 of Coagulation factor VII
5l0s B 55 B 81
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 115 and 141 (55 and 81 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
5l0s
Structure name
human poglut1 in complex with factor vii egf1 and udp
Structure deposition date
2016-07-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
115
Residue number B
141
Peptide name
Coagulation factor VII
Ligandability
Cysteine 115 of Coagulation factor VII
Cysteine 141 of Coagulation factor VII
1w8b L 91 L 112
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 151 and 172 (91 and 112 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
1w8b
Structure name
factor7 - 413 complex
Structure deposition date
2004-09-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
151
Residue number B
172
Peptide name
Coagulation factor VII
Ligandability
Cysteine 151 of Coagulation factor VII
Cysteine 172 of Coagulation factor VII
2c4f L 55 L 72
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 115 and 132 (55 and 72 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
2c4f
Structure name
crystal structure of factor vii
Structure deposition date
2005-10-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
115
Residue number B
132
Peptide name
Coagulation factor VII
Ligandability
Cysteine 115 of Coagulation factor VII
Cysteine 132 of Coagulation factor VII
1w7x L 112 L 127
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 172 and 187 (112 and 127 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
1w7x
Structure name
factor7 - 413 complex
Structure deposition date
2004-09-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
172
Residue number B
187
Peptide name
Coagulation factor VII
Ligandability
Cysteine 172 of Coagulation factor VII
Cysteine 187 of Coagulation factor VII
5ky2 B 91 B 111
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 91 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5ky2
Structure name
mouse pofut1 in complex with o-glucosylated mouse factor vii egf1 and gdp
Structure deposition date
2016-07-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P70375
Residue number A
91
Residue number B
111
Peptide name
Coagulation factor VII
Ligandability
Cysteine 91 of Coagulation factor VII
Cysteine 111 of Coagulation factor VII
1fak L 98 L 127
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 158 and 187 (98 and 127 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
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)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
158
Residue number B
187
Peptide name
Coagulation factor VII
Ligandability
Cysteine 158 of Coagulation factor VII
Cysteine 187 of Coagulation factor VII
1f7e A 61 A 72
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 121 and 132 (61 and 72 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
1f7e
Structure name
the first egf-like domain from human blood coagulation fvii, nmr, 20 structures
Structure deposition date
1999-02-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
121
Residue number B
132
Peptide name
Coagulation factor VII
Ligandability
Cysteine 121 of Coagulation factor VII
Cysteine 132 of Coagulation factor VII
2b8o L 112 L 114
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 172 and 174 (112 and 114 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
2b8o
Structure name
crystal structure of glu-gly-arg-chloromethyl ketone-factor viia/soluble tissue factor complex
Structure deposition date
2005-10-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
172
Residue number B
174
Peptide name
Coagulation factor VII
Ligandability
Cysteine 172 of Coagulation factor VII
Cysteine 174 of Coagulation factor VII
2f9b L 61 L 81
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 121 and 141 (61 and 81 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
2f9b
Structure name
discovery of novel heterocyclic factor viia inhibitors
Structure deposition date
2005-12-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
121
Residue number B
141
Peptide name
Coagulation factor VII
Ligandability
Cysteine 121 of Coagulation factor VII
Cysteine 141 of Coagulation factor VII
2flr L 98 L 114
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 158 and 174 (98 and 114 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
2flr
Structure name
novel 5-azaindole factor viia inhibitors
Structure deposition date
2006-01-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
158
Residue number B
174
Peptide name
Coagulation factor VII
Ligandability
Cysteine 158 of Coagulation factor VII
Cysteine 174 of Coagulation factor VII
1ff7 A 50 A 72
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 110 and 132 (50 and 72 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
1ff7
Structure name
the first egf-like domain from human blood coagulation fvii (fucosylated at ser-60), nmr, 20 structures
Structure deposition date
1999-02-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
110
Residue number B
132
Peptide name
Coagulation factor VII
Ligandability
Cysteine 110 of Coagulation factor VII
Cysteine 132 of Coagulation factor VII
1ff7 A 50 A 81
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 110 and 141 (50 and 81 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
1ff7
Structure name
the first egf-like domain from human blood coagulation fvii (fucosylated at ser-60), nmr, 20 structures
Structure deposition date
1999-02-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
110
Residue number B
141
Peptide name
Coagulation factor VII
Ligandability
Cysteine 110 of Coagulation factor VII
Cysteine 141 of Coagulation factor VII
1cvw L 127 L 135
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 187 and 195 (127 and 135 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
1cvw
Structure name
crystal structure of active site-inhibited human coagulation factor viia (des-gla)
Structure deposition date
1999-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
187
Residue number B
195
Peptide name
Coagulation factor VII
Ligandability
Cysteine 187 of Coagulation factor VII
Cysteine 195 of Coagulation factor VII
1jbu H 42 H 220
A redox-regulated disulphide may form within Coagulation factor VII between cysteines 238 and 428 (42 and 220 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1jbu
Structure name
coagulation factor vii zymogen (egf2/protease) in complex with inhibitory exosite peptide a-183
Structure deposition date
2001-06-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08709
Residue number A
238
Residue number B
428
Peptide name
Coagulation factor VII
Ligandability
Cysteine 238 of Coagulation factor VII
Cysteine 428 of Coagulation factor VII
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