Vascular endothelial growth factor C
Intermolecular
Cysteine 165 and cysteine 156
Cysteine 166 and cysteine 156
Cysteine 156 and cysteine 211
Intramolecular
Cysteine 162 and cysteine 209
Cysteine 131 and cysteine 173
Cysteine 166 and cysteine 211
Cysteine 173 and cysteine 209
Cysteine 131 and cysteine 209
Cysteine 131 and cysteine 211
Cysteine 131 and cysteine 166
More...Cysteine 166 and cysteine 173
Cysteine 162 and cysteine 173
Cysteine 173 and cysteine 211
Cysteine 131 and cysteine 162
Cysteine 165 and cysteine 166
Cysteine 209 and cysteine 211
Cysteine 165 and cysteine 211
Cysteine 165 and cysteine 173
Cysteine 162 and cysteine 211
Cysteine 131 and cysteine 165
Cysteine 166 and cysteine 209
Cysteine 162 and cysteine 166
2x1w C 165 D 156
A redox-regulated disulphide may form between two units of Vascular endothelial growth factor C at cysteines 165 and 156.
Details
Redox score ?
78
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide A name
Vascular endothelial growth factor C
Peptide B name
Vascular endothelial growth factor C
Peptide A accession
P49767
Peptide B accession
P49767
Peptide A residue number
165
Peptide B residue number
156
Ligandability
Cysteine 165 of Vascular endothelial growth factor C
Cysteine 156 of Vascular endothelial growth factor C
2x1w C 166 D 156
A redox-regulated disulphide may form between two units of Vascular endothelial growth factor C at cysteines 166 and 156. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Vascular endothelial growth factor C
Peptide B name
Vascular endothelial growth factor C
Peptide A accession
P49767
Peptide B accession
P49767
Peptide A residue number
166
Peptide B residue number
156
Ligandability
Cysteine 166 of Vascular endothelial growth factor C
Cysteine 156 of Vascular endothelial growth factor C
2x1w C 156 D 211
A redox-regulated disulphide may form between two units of Vascular endothelial growth factor C at cysteines 156 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Vascular endothelial growth factor C
Peptide B name
Vascular endothelial growth factor C
Peptide A accession
P49767
Peptide B accession
P49767
Peptide A residue number
156
Peptide B residue number
211
Ligandability
Cysteine 156 of Vascular endothelial growth factor C
Cysteine 211 of Vascular endothelial growth factor C
2x1x E 162 E 209
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 162 and 209.
Details
Redox score ?
88
PDB code
2x1x
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2 in a tetragonal crystal form
Structure deposition date
2010-01-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
162
Residue number B
209
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 162 of Vascular endothelial growth factor C
Cysteine 209 of Vascular endothelial growth factor C
2x1w C 131 C 173
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 131 and 173.
Details
Redox score ?
84
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
131
Residue number B
173
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 131 of Vascular endothelial growth factor C
Cysteine 173 of Vascular endothelial growth factor C
2x1w A 166 A 211
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 166 and 211.
Details
Redox score ?
83
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
166
Residue number B
211
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 166 of Vascular endothelial growth factor C
Cysteine 211 of Vascular endothelial growth factor C
4bsk C 173 C 209
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 173 and 209.
Details
Redox score ?
73
PDB code
4bsk
Structure name
crystal structure of vegf-c in complex with vegfr-3 domains d1-2
Structure deposition date
2013-06-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
173
Residue number B
209
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 173 of Vascular endothelial growth factor C
Cysteine 209 of Vascular endothelial growth factor C
4bsk C 131 C 209
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 131 and 209.
Details
Redox score ?
72
PDB code
4bsk
Structure name
crystal structure of vegf-c in complex with vegfr-3 domains d1-2
Structure deposition date
2013-06-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
131
Residue number B
209
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 131 of Vascular endothelial growth factor C
Cysteine 209 of Vascular endothelial growth factor C
2x1w B 131 B 211
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 131 and 211.
Details
Redox score ?
71
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
131
Residue number B
211
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 131 of Vascular endothelial growth factor C
Cysteine 211 of Vascular endothelial growth factor C
2x1x E 131 E 166
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 131 and 166.
Details
Redox score ?
70
PDB code
2x1x
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2 in a tetragonal crystal form
Structure deposition date
2010-01-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
131
Residue number B
166
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 131 of Vascular endothelial growth factor C
Cysteine 166 of Vascular endothelial growth factor C
4bsk C 166 C 173
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 166 and 173.
Details
Redox score ?
70
PDB code
4bsk
Structure name
crystal structure of vegf-c in complex with vegfr-3 domains d1-2
Structure deposition date
2013-06-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
166
Residue number B
173
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 166 of Vascular endothelial growth factor C
Cysteine 173 of Vascular endothelial growth factor C
2x1w A 162 A 173
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 162 and 173.
Details
Redox score ?
69
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
162
Residue number B
173
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 162 of Vascular endothelial growth factor C
Cysteine 173 of Vascular endothelial growth factor C
2x1w B 173 B 211
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 173 and 211.
Details
Redox score ?
67
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
173
Residue number B
211
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 173 of Vascular endothelial growth factor C
Cysteine 211 of Vascular endothelial growth factor C
2x1x E 131 E 162
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 131 and 162.
Details
Redox score ?
66
PDB code
2x1x
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2 in a tetragonal crystal form
Structure deposition date
2010-01-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
131
Residue number B
162
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 131 of Vascular endothelial growth factor C
Cysteine 162 of Vascular endothelial growth factor C
4bsk C 165 C 166
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 165 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
4bsk
Structure name
crystal structure of vegf-c in complex with vegfr-3 domains d1-2
Structure deposition date
2013-06-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
nan
Peptide accession
P49767
Residue number A
165
Residue number B
166
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 165 of Vascular endothelial growth factor C
Cysteine 166 of Vascular endothelial growth factor C
2x1w B 209 B 211
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 209 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
209
Residue number B
211
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 209 of Vascular endothelial growth factor C
Cysteine 211 of Vascular endothelial growth factor C
2x1w B 165 B 211
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 165 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
165
Residue number B
211
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 165 of Vascular endothelial growth factor C
Cysteine 211 of Vascular endothelial growth factor C
2x1w B 165 B 173
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 165 and 173. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
165
Residue number B
173
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 165 of Vascular endothelial growth factor C
Cysteine 173 of Vascular endothelial growth factor C
2x1w B 162 B 211
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 162 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
162
Residue number B
211
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 162 of Vascular endothelial growth factor C
Cysteine 211 of Vascular endothelial growth factor C
2x1x E 131 E 165
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 131 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2x1x
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2 in a tetragonal crystal form
Structure deposition date
2010-01-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
nan
Peptide accession
P49767
Residue number A
131
Residue number B
165
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 131 of Vascular endothelial growth factor C
Cysteine 165 of Vascular endothelial growth factor C
2x1w D 166 D 209
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 166 and 209. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
166
Residue number B
209
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 166 of Vascular endothelial growth factor C
Cysteine 209 of Vascular endothelial growth factor C
2x1w C 162 C 166
A redox-regulated disulphide may form within Vascular endothelial growth factor C between cysteines 162 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
2x1w
Structure name
crystal structure of vegf-c in complex with domains 2 and 3 of vegfr2
Structure deposition date
2010-01-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P49767
Residue number A
162
Residue number B
166
Peptide name
Vascular endothelial growth factor C
Ligandability
Cysteine 162 of Vascular endothelial growth factor C
Cysteine 166 of Vascular endothelial growth factor C
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