Coagulation factor X
Intermolecular
Cysteine 172 and cysteine 342
Cysteine 261 and cysteine 70 of Ecotin
Cysteine 442 and cysteine 5 of Tick anticoagulant peptide
Cysteine 261 and cysteine 65 of Anti-coagulant protein 5
Cysteine 342 and cysteine 164
Cysteine 415 and cysteine 38 of Anti-coagulant protein 5
Cysteine 277 and cysteine 70 of Ecotin
Intramolecular
Cysteine 57 and cysteine 62
Cysteine 112 and cysteine 121
Cysteine 136 and cysteine 149
More...Cysteine 90 and cysteine 101
Cysteine 129 and cysteine 140
Cysteine 151 and cysteine 164
Cysteine 241 and cysteine 246
Cysteine 95 and cysteine 110
Cysteine 390 and cysteine 404
Cysteine 415 and cysteine 443
Cysteine 95 and cysteine 101
Cysteine 261 and cysteine 277
Cysteine 110 and cysteine 121
Cysteine 101 and cysteine 110
Cysteine 136 and cysteine 140
Cysteine 140 and cysteine 149
Cysteine 95 and cysteine 121
Cysteine 89 and cysteine 136
Cysteine 90 and cysteine 95
Cysteine 129 and cysteine 136
Cysteine 90 and cysteine 95
Cysteine 95 and cysteine 112
Cysteine 89 and cysteine 149
Cysteine 129 and cysteine 149
Cysteine 149 and cysteine 164
Cysteine 110 and cysteine 112
Cysteine 136 and cysteine 164
Cysteine 149 and cysteine 151
Cysteine 90 and cysteine 110
Cysteine 101 and cysteine 121
Cysteine 136 and cysteine 151
Cysteine 101 and cysteine 112
Cysteine 164 and cysteine 172
2bq6 A 44 B 122
A redox-regulated disulphide may form between two units of Coagulation factor X at cysteines 172 and 342 (44 and 122 respectively in this structure).
Details
Redox score ?
78
PDB code
2bq6
Structure name
crystal structure of factor xa in complex with 21
Structure deposition date
2005-04-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Coagulation factor X
Peptide A accession
P00742
Peptide B accession
P00742
Peptide A residue number
172
Peptide B residue number
342
Ligandability
Cysteine 172 of Coagulation factor X
Cysteine 342 of Coagulation factor X
1p0s H 42 E 50
A redox-regulated disulphide may form between cysteine 261 of Coagulation factor X and cysteine 70 of Ecotin (42 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1p0s
Structure name
crystal structure of blood coagulation factor xa in complex with ecotin m84r
Structure deposition date
2003-04-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Ecotin
Peptide A accession
P00742
Peptide B accession
P23827
Peptide A residue number
261
Peptide B residue number
70
Ligandability
Cysteine 261 of Coagulation factor X
Cysteine 70 of Ecotin
1kig H 220 I 505
A redox-regulated disulphide may form between cysteine 442 of Coagulation factor X and cysteine 5 of Tick anticoagulant peptide (220 and 505 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
1kig
Structure name
bovine factor xa
Structure deposition date
1997-04-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Tick anticoagulant peptide
Peptide A accession
P00743
Peptide B accession
P17726
Peptide A residue number
442
Peptide B residue number
5
Ligandability
Cysteine 442 of Coagulation factor X
Cysteine 5 of Tick anticoagulant peptide
2p3f H 42 N 42
A redox-regulated disulphide may form between cysteine 261 of Coagulation factor X and cysteine 65 of Anti-coagulant protein 5 (42 and 42 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
2p3f
Structure name
crystal structure of the factor xa/nap5 complex
Structure deposition date
2007-03-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Anti-coagulant protein 5
Peptide A accession
P00742
Peptide B accession
Q16940
Peptide A residue number
261
Peptide B residue number
65
Ligandability
Cysteine 261 of Coagulation factor X
Cysteine 65 of Anti-coagulant protein 5
2cji A 122 B 36
A redox-regulated disulphide may form between two units of Coagulation factor X at cysteines 342 and 164 (122 and 36 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
2cji
Structure name
crystal structure of a human factor xa inhibitor complex
Structure deposition date
2006-04-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Coagulation factor X
Peptide A accession
P00742
Peptide B accession
P00742
Peptide A residue number
342
Peptide B residue number
164
Ligandability
Cysteine 342 of Coagulation factor X
Cysteine 164 of Coagulation factor X
2p3f H 191 N 15
A redox-regulated disulphide may form between cysteine 415 of Coagulation factor X and cysteine 38 of Anti-coagulant protein 5 (191 and 15 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
2p3f
Structure name
crystal structure of the factor xa/nap5 complex
Structure deposition date
2007-03-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Anti-coagulant protein 5
Peptide A accession
P00742
Peptide B accession
Q16940
Peptide A residue number
415
Peptide B residue number
38
Ligandability
Cysteine 415 of Coagulation factor X
Cysteine 38 of Anti-coagulant protein 5
1p0s H 58 E 50
A redox-regulated disulphide may form between cysteine 277 of Coagulation factor X and cysteine 70 of Ecotin (58 and 50 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
1p0s
Structure name
crystal structure of blood coagulation factor xa in complex with ecotin m84r
Structure deposition date
2003-04-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide A name
Coagulation factor X
Peptide B name
Ecotin
Peptide A accession
P00742
Peptide B accession
P23827
Peptide A residue number
277
Peptide B residue number
70
Ligandability
Cysteine 277 of Coagulation factor X
Cysteine 70 of Ecotin
1p0s L 17 L 22
A redox-regulated disulphide may form within Coagulation factor X between cysteines 57 and 62 (17 and 22 respectively in this structure).
Details
Redox score ?
90
PDB code
1p0s
Structure name
crystal structure of blood coagulation factor xa in complex with ecotin m84r
Structure deposition date
2003-04-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
57
Residue number B
62
Peptide name
Coagulation factor X
Ligandability
Cysteine 57 of Coagulation factor X
Cysteine 62 of Coagulation factor X
3hpt C 112 C 121
A redox-regulated disulphide may form within Coagulation factor X between cysteines 112 and 121.
Details
Redox score ?
88
PDB code
3hpt
Structure name
crystal structure of human fxa in complex with (s)-2-cyano-1-(2- methylbenzofuran-5-yl)-3-(2-oxo-1-(2-oxo-2-(pyrrolidin-1-yl)ethyl) azepan-3-yl)guanidine
Structure deposition date
2009-06-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
112
Residue number B
121
Peptide name
Coagulation factor X
Ligandability
Cysteine 112 of Coagulation factor X
Cysteine 121 of Coagulation factor X
2j95 B 8 B 21
A redox-regulated disulphide may form within Coagulation factor X between cysteines 136 and 149 (8 and 21 respectively in this structure).
Details
Redox score ?
87
PDB code
2j95
Structure name
crystal structure of a human factor xa inhibitor complex
Structure deposition date
2006-11-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
136
Residue number B
149
Peptide name
Coagulation factor X
Ligandability
Cysteine 136 of Coagulation factor X
Cysteine 149 of Coagulation factor X
1apo A 50 A 61
A redox-regulated disulphide may form within Coagulation factor X between cysteines 90 and 101 (50 and 61 respectively in this structure).
Details
Redox score ?
86
PDB code
1apo
Structure name
three-dimensional structure of the apo form of the n-terminal egf-like module of blood coagulation factor x as determined by nmr spectroscopy and simulated folding
Structure deposition date
1992-04-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00743
Residue number A
90
Residue number B
101
Peptide name
Coagulation factor X
Ligandability
Cysteine 90 of Coagulation factor X
Cysteine 101 of Coagulation factor X
1xkb A 89 A 100
A redox-regulated disulphide may form within Coagulation factor X between cysteines 129 and 140 (89 and 100 respectively in this structure).
Details
Redox score ?
86
PDB code
1xkb
Structure name
factor xa complexed with a synthetic inhibitor fx-2212a,(2s)-(3'- amidino-3-biphenylyl)-5-(4-pyridylamino)pentanoic acid
Structure deposition date
1998-03-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
129
Residue number B
140
Peptide name
Coagulation factor X
Ligandability
Cysteine 129 of Coagulation factor X
Cysteine 140 of Coagulation factor X
2p3u A 111 A 124
A redox-regulated disulphide may form within Coagulation factor X between cysteines 151 and 164 (111 and 124 respectively in this structure).
Details
Redox score ?
86
PDB code
2p3u
Structure name
crystal structure of human factor xa complexed with 3- chloro-n-(4-chloro-2-{[(5-chloropyridin-2-yl) amino]carbonyl}-6-methoxyphenyl)-4-[(1-methyl-1h-imidazol- 2-yl)methyl]thiophene-2-carboxamide {pfizer 320663}
Structure deposition date
2007-03-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
151
Residue number B
164
Peptide name
Coagulation factor X
Ligandability
Cysteine 151 of Coagulation factor X
Cysteine 164 of Coagulation factor X
2bq7 B 22 B 27
A redox-regulated disulphide may form within Coagulation factor X between cysteines 241 and 246 (22 and 27 respectively in this structure).
Details
Redox score ?
83
PDB code
2bq7
Structure name
crystal structure of factor xa in complex with 43
Structure deposition date
2005-04-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
241
Residue number B
246
Peptide name
Coagulation factor X
Ligandability
Cysteine 241 of Coagulation factor X
Cysteine 246 of Coagulation factor X
7tpq A 55 A 70
A redox-regulated disulphide may form within Coagulation factor X between cysteines 95 and 110 (55 and 70 respectively in this structure).
Details
Redox score ?
82
PDB code
7tpq
Structure name
cryo-em structure of human prothrombinase on a nanodisc at 5
Structure deposition date
2022-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
P00742
Residue number A
95
Residue number B
110
Peptide name
Coagulation factor X
Ligandability
Cysteine 95 of Coagulation factor X
Cysteine 110 of Coagulation factor X
2p95 A 168 A 182
A redox-regulated disulphide may form within Coagulation factor X between cysteines 390 and 404 (168 and 182 respectively in this structure).
Details
Redox score ?
81
PDB code
2p95
Structure name
factor xa in complex with the inhibitor 5-chloro-n-((1r,2s)-2-(4-(2- oxopyridin-1(2h)-yl)benzamido) cyclopentyl)thiophene-2-carboxamide
Structure deposition date
2007-03-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
76
Minimum pKa ?
7
% buried
62
Peptide accession
P00742
Residue number A
390
Residue number B
404
Peptide name
Coagulation factor X
Ligandability
Cysteine 390 of Coagulation factor X
Cysteine 404 of Coagulation factor X
1nfy A 191 A 220
A redox-regulated disulphide may form within Coagulation factor X between cysteines 415 and 443 (191 and 220 respectively in this structure).
Details
Redox score ?
79
PDB code
1nfy
Structure name
crystal structure of human coagulation factor xa complexed with rpr200095
Structure deposition date
2002-12-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
415
Residue number B
443
Peptide name
Coagulation factor X
Ligandability
Cysteine 415 of Coagulation factor X
Cysteine 443 of Coagulation factor X
1xka L 55 L 61
A redox-regulated disulphide may form within Coagulation factor X between cysteines 95 and 101 (55 and 61 respectively in this structure).
Details
Redox score ?
79
PDB code
1xka
Structure name
factor xa complexed with a synthetic inhibitor fx-2212a,(2s)-(3'- amidino-3-biphenylyl)-5-(4-pyridylamino)pentanoic acid
Structure deposition date
1998-03-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
95
Residue number B
101
Peptide name
Coagulation factor X
Ligandability
Cysteine 95 of Coagulation factor X
Cysteine 101 of Coagulation factor X
1p0s H 42 H 58
A redox-regulated disulphide may form within Coagulation factor X between cysteines 261 and 277 (42 and 58 respectively in this structure).
Details
Redox score ?
78
PDB code
1p0s
Structure name
crystal structure of blood coagulation factor xa in complex with ecotin m84r
Structure deposition date
2003-04-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
104
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
261
Residue number B
277
Peptide name
Coagulation factor X
Ligandability
Cysteine 261 of Coagulation factor X
Cysteine 277 of Coagulation factor X
1apo A 70 A 81
A redox-regulated disulphide may form within Coagulation factor X between cysteines 110 and 121 (70 and 81 respectively in this structure).
Details
Redox score ?
77
PDB code
1apo
Structure name
three-dimensional structure of the apo form of the n-terminal egf-like module of blood coagulation factor x as determined by nmr spectroscopy and simulated folding
Structure deposition date
1992-04-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
0
Peptide accession
P00743
Residue number A
110
Residue number B
121
Peptide name
Coagulation factor X
Ligandability
Cysteine 110 of Coagulation factor X
Cysteine 121 of Coagulation factor X
1xkb B 61 B 70
A redox-regulated disulphide may form within Coagulation factor X between cysteines 101 and 110 (61 and 70 respectively in this structure).
Details
Redox score ?
76
PDB code
1xkb
Structure name
factor xa complexed with a synthetic inhibitor fx-2212a,(2s)-(3'- amidino-3-biphenylyl)-5-(4-pyridylamino)pentanoic acid
Structure deposition date
1998-03-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
101
Residue number B
110
Peptide name
Coagulation factor X
Ligandability
Cysteine 101 of Coagulation factor X
Cysteine 110 of Coagulation factor X
2p16 L 96 L 100
A redox-regulated disulphide may form within Coagulation factor X between cysteines 136 and 140 (96 and 100 respectively in this structure).
Details
Redox score ?
73
PDB code
2p16
Structure name
factor xa in complex with the inhibitor apixaban (bms- 562247) aka 1-(4-methoxyphenyl)-7-oxo-6-(4-(2-oxo-1- piperidinyl)phenyl)-4,5,6,7-tetrahydro-1h-pyrazolo[3, 4- c]pyridine-3-carboxamide
Structure deposition date
2007-03-02
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
nan
Peptide accession
P00742
Residue number A
136
Residue number B
140
Peptide name
Coagulation factor X
Ligandability
Cysteine 136 of Coagulation factor X
Cysteine 140 of Coagulation factor X
1p0s L 100 L 109
A redox-regulated disulphide may form within Coagulation factor X between cysteines 140 and 149 (100 and 109 respectively in this structure).
Details
Redox score ?
71
PDB code
1p0s
Structure name
crystal structure of blood coagulation factor xa in complex with ecotin m84r
Structure deposition date
2003-04-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
140
Residue number B
149
Peptide name
Coagulation factor X
Ligandability
Cysteine 140 of Coagulation factor X
Cysteine 149 of Coagulation factor X
3ens A 95 A 121
A redox-regulated disulphide may form within Coagulation factor X between cysteines 95 and 121.
Details
Redox score ?
69
PDB code
3ens
Structure name
crystal structure of human fxa in complex with methyl (2z)-3-[(3- chloro-1h-indol-7-yl)amino]-2-cyano-3-{[(3s)-2-oxo-1-(2-oxo-2- pyrrolidin-1-ylethyl)azepan-3-yl]amino}acrylate
Structure deposition date
2008-09-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
95
Residue number B
121
Peptide name
Coagulation factor X
Ligandability
Cysteine 95 of Coagulation factor X
Cysteine 121 of Coagulation factor X
2vwl L 89 L 96
A redox-regulated disulphide may form within Coagulation factor X between cysteines 89 and 136 (89 and 96 respectively in this structure).
Details
Redox score ?
68
PDB code
2vwl
Structure name
aminopyrrolidine factor xa inhibitor
Structure deposition date
2008-06-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
89
Residue number B
136
Peptide name
Coagulation factor X
Ligandability
Cysteine 89 of Coagulation factor X
Cysteine 136 of Coagulation factor X
Cysteine 89 in protein A could not be asigned to a Uniprot residue.
3hpt A 90 A 95
A redox-regulated disulphide may form within Coagulation factor X between cysteines 90 and 95.
Details
Redox score ?
68
PDB code
3hpt
Structure name
crystal structure of human fxa in complex with (s)-2-cyano-1-(2- methylbenzofuran-5-yl)-3-(2-oxo-1-(2-oxo-2-(pyrrolidin-1-yl)ethyl) azepan-3-yl)guanidine
Structure deposition date
2009-06-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
90
Residue number B
95
Peptide name
Coagulation factor X
Ligandability
Cysteine 90 of Coagulation factor X
Cysteine 95 of Coagulation factor X
Cysteine 90 in protein A could not be asigned to a Uniprot residue.
2vvu L 89 L 96
A redox-regulated disulphide may form within Coagulation factor X between cysteines 129 and 136 (89 and 96 respectively in this structure).
Details
Redox score ?
67
PDB code
2vvu
Structure name
aminopyrrolidine factor xa inhibitor
Structure deposition date
2008-06-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
129
Residue number B
136
Peptide name
Coagulation factor X
Ligandability
Cysteine 129 of Coagulation factor X
Cysteine 136 of Coagulation factor X
1whe A 50 A 55
A redox-regulated disulphide may form within Coagulation factor X between cysteines 90 and 95 (50 and 55 respectively in this structure).
Details
Redox score ?
66
PDB code
1whe
Structure name
coagulation factor, nmr, 20 structures
Structure deposition date
1996-06-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00743
Residue number A
90
Residue number B
95
Peptide name
Coagulation factor X
Ligandability
Cysteine 90 of Coagulation factor X
Cysteine 95 of Coagulation factor X
3hpt C 95 C 112
A redox-regulated disulphide may form within Coagulation factor X between cysteines 95 and 112.
Details
Redox score ?
60
PDB code
3hpt
Structure name
crystal structure of human fxa in complex with (s)-2-cyano-1-(2- methylbenzofuran-5-yl)-3-(2-oxo-1-(2-oxo-2-(pyrrolidin-1-yl)ethyl) azepan-3-yl)guanidine
Structure deposition date
2009-06-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
95
Residue number B
112
Peptide name
Coagulation factor X
Ligandability
Cysteine 95 of Coagulation factor X
Cysteine 112 of Coagulation factor X
2vwl L 89 L 109
A redox-regulated disulphide may form within Coagulation factor X between cysteines 89 and 149 (89 and 109 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
2vwl
Structure name
aminopyrrolidine factor xa inhibitor
Structure deposition date
2008-06-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
89
Residue number B
149
Peptide name
Coagulation factor X
Ligandability
Cysteine 89 of Coagulation factor X
Cysteine 149 of Coagulation factor X
Cysteine 89 in protein A could not be asigned to a Uniprot residue.
4bti A 1 A 21
A redox-regulated disulphide may form within Coagulation factor X between cysteines 129 and 149 (1 and 21 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
4bti
Structure name
factor xa in complex with the dual thrombin-fxa inhibitor 58
Structure deposition date
2013-06-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
129
Residue number B
149
Peptide name
Coagulation factor X
Ligandability
Cysteine 129 of Coagulation factor X
Cysteine 149 of Coagulation factor X
2vwl L 109 L 124
A redox-regulated disulphide may form within Coagulation factor X between cysteines 149 and 164 (109 and 124 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2vwl
Structure name
aminopyrrolidine factor xa inhibitor
Structure deposition date
2008-06-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
149
Residue number B
164
Peptide name
Coagulation factor X
Ligandability
Cysteine 149 of Coagulation factor X
Cysteine 164 of Coagulation factor X
1ccf A 70 A 72
A redox-regulated disulphide may form within Coagulation factor X between cysteines 110 and 112 (70 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 ?
54
PDB code
1ccf
Structure name
how an epidermal growth factor (egf)-like domain binds calcium-high resolution nmr structure of the calcium form of the nh2-terminal egf- like domain in coagulation factor x
Structure deposition date
1993-05-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00743
Residue number A
110
Residue number B
112
Peptide name
Coagulation factor X
Ligandability
Cysteine 110 of Coagulation factor X
Cysteine 112 of Coagulation factor X
2p3f L 96 L 124
A redox-regulated disulphide may form within Coagulation factor X between cysteines 136 and 164 (96 and 124 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
2p3f
Structure name
crystal structure of the factor xa/nap5 complex
Structure deposition date
2007-03-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
136
Residue number B
164
Peptide name
Coagulation factor X
Ligandability
Cysteine 136 of Coagulation factor X
Cysteine 164 of Coagulation factor X
1p0s L 109 L 111
A redox-regulated disulphide may form within Coagulation factor X between cysteines 149 and 151 (109 and 111 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
1p0s
Structure name
crystal structure of blood coagulation factor xa in complex with ecotin m84r
Structure deposition date
2003-04-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
149
Residue number B
151
Peptide name
Coagulation factor X
Ligandability
Cysteine 149 of Coagulation factor X
Cysteine 151 of Coagulation factor X
1apo A 50 A 70
A redox-regulated disulphide may form within Coagulation factor X between cysteines 90 and 110 (50 and 70 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
1apo
Structure name
three-dimensional structure of the apo form of the n-terminal egf-like module of blood coagulation factor x as determined by nmr spectroscopy and simulated folding
Structure deposition date
1992-04-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00743
Residue number A
90
Residue number B
110
Peptide name
Coagulation factor X
Ligandability
Cysteine 90 of Coagulation factor X
Cysteine 110 of Coagulation factor X
3hpt C 101 C 121
A redox-regulated disulphide may form within Coagulation factor X between cysteines 101 and 121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3hpt
Structure name
crystal structure of human fxa in complex with (s)-2-cyano-1-(2- methylbenzofuran-5-yl)-3-(2-oxo-1-(2-oxo-2-(pyrrolidin-1-yl)ethyl) azepan-3-yl)guanidine
Structure deposition date
2009-06-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
101
Residue number B
121
Peptide name
Coagulation factor X
Ligandability
Cysteine 101 of Coagulation factor X
Cysteine 121 of Coagulation factor X
3m37 L 96 L 111
A redox-regulated disulphide may form within Coagulation factor X between cysteines 136 and 151 (96 and 111 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
3m37
Structure name
factor xa in complex with the inhibitor 1-[2-(aminomethyl) phenyl]-n-(3-fluoro-2'-sulfamoylbiphenyl-4-yl)-3- (trifluoromethyl)-1h-pyrazole-5-carboxamide (dpc602)
Structure deposition date
2010-03-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
nan
Peptide accession
P00742
Residue number A
136
Residue number B
151
Peptide name
Coagulation factor X
Ligandability
Cysteine 136 of Coagulation factor X
Cysteine 151 of Coagulation factor X
1ccf A 61 A 72
A redox-regulated disulphide may form within Coagulation factor X between cysteines 101 and 112 (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 ?
43
PDB code
1ccf
Structure name
how an epidermal growth factor (egf)-like domain binds calcium-high resolution nmr structure of the calcium form of the nh2-terminal egf- like domain in coagulation factor x
Structure deposition date
1993-05-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00743
Residue number A
101
Residue number B
112
Peptide name
Coagulation factor X
Ligandability
Cysteine 101 of Coagulation factor X
Cysteine 112 of Coagulation factor X
4btu E 36 E 44
A redox-regulated disulphide may form within Coagulation factor X between cysteines 164 and 172 (36 and 44 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
4btu
Structure name
factor xa in complex with the dual thrombin-fxa inhibitor 57
Structure deposition date
2013-06-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00742
Residue number A
164
Residue number B
172
Peptide name
Coagulation factor X
Ligandability
Cysteine 164 of Coagulation factor X
Cysteine 172 of Coagulation factor X
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