Vascular endothelial growth factor receptor 2
Intermolecular
Cysteine 862 and cysteine 862
Intramolecular
Cysteine 740 and cysteine 745
Cysteine 466 and cysteine 482
Cysteine 246 and cysteine 307
Cysteine 150 and cysteine 200
Cysteine 688 and cysteine 737
Cysteine 445 and cysteine 530
Cysteine 817 and cysteine 1024
Cysteine 919 and cysteine 1045
Cysteine 162 and cysteine 200
Cysteine 150 and cysteine 162
2p2i A 862 B 862
A redox-regulated disulphide may form between two units of Vascular endothelial growth factor receptor 2 at cysteines 862 and 862. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
2p2i
Structure name
crystal structure of the vegfr2 kinase domain in complex with a nicotinamide inhibitor
Structure deposition date
2007-03-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
10
% buried
22
Peptide A name
Vascular endothelial growth factor receptor 2
Peptide B name
Vascular endothelial growth factor receptor 2
Peptide A accession
P35968
Peptide B accession
P35968
Peptide A residue number
862
Peptide B residue number
862
Ligandability
3kvq A 740 A 745
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 740 and 745.
Details
Redox score ?
94
PDB code
3kvq
Structure name
crystal structure of vegfr2 extracellular domain d7
Structure deposition date
2009-11-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
0
Peptide accession
P35968
Residue number A
740
Residue number B
745
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 740 of Vascular endothelial growth factor receptor 2
Cysteine 745 of Vascular endothelial growth factor receptor 2
5oyj C 466 C 482
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 466 and 482.
Details
Redox score ?
89
PDB code
5oyj
Structure name
crystal structure of vegfr-2 domains 4-5 in complex with darpin d4b
Structure deposition date
2017-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35968
Residue number A
466
Residue number B
482
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 466 of Vascular endothelial growth factor receptor 2
Cysteine 482 of Vascular endothelial growth factor receptor 2
3v2a R 246 R 307
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 246 and 307.
Details
Redox score ?
82
PDB code
3v2a
Structure name
vegfr-2/vegf-a complex structure
Structure deposition date
2011-12-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35968
Residue number A
246
Residue number B
307
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 246 of Vascular endothelial growth factor receptor 2
Cysteine 307 of Vascular endothelial growth factor receptor 2
2x1x R 150 R 200
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 150 and 200.
Details
Redox score ?
82
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 ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35968
Residue number A
150
Residue number B
200
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 150 of Vascular endothelial growth factor receptor 2
Cysteine 200 of Vascular endothelial growth factor receptor 2
3kvq A 688 A 737
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 688 and 737.
Details
Redox score ?
81
PDB code
3kvq
Structure name
crystal structure of vegfr2 extracellular domain d7
Structure deposition date
2009-11-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35968
Residue number A
688
Residue number B
737
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 688 of Vascular endothelial growth factor receptor 2
Cysteine 737 of Vascular endothelial growth factor receptor 2
5oyj D 445 D 530
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 445 and 530.
Details
Redox score ?
79
PDB code
5oyj
Structure name
crystal structure of vegfr-2 domains 4-5 in complex with darpin d4b
Structure deposition date
2017-09-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35968
Residue number A
445
Residue number B
530
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 445 of Vascular endothelial growth factor receptor 2
Cysteine 530 of Vascular endothelial growth factor receptor 2
3vhe A 817 A 1024
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 817 and 1024. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3vhe
Structure name
crystal structure of human vegfr2 kinase domain with a novel pyrrolopyrimidine inhibitor
Structure deposition date
2011-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
42
Peptide accession
P35968
Residue number A
817
Residue number B
1024
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 817 of Vascular endothelial growth factor receptor 2
Cysteine 1024 of Vascular endothelial growth factor receptor 2
3cpc B 919 B 1045
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 919 and 1045. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3cpc
Structure name
crystal structure of the vegfr2 kinase domain in complex with a pyridone inhibitor
Structure deposition date
2008-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
96
Peptide accession
P35968
Residue number A
919
Residue number B
1045
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 919 of Vascular endothelial growth factor receptor 2
Cysteine 1045 of Vascular endothelial growth factor receptor 2
2x1w N 162 N 200
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 162 and 200. 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)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35968
Residue number A
162
Residue number B
200
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 162 of Vascular endothelial growth factor receptor 2
Cysteine 200 of Vascular endothelial growth factor receptor 2
2x1w M 150 M 162
A redox-regulated disulphide may form within Vascular endothelial growth factor receptor 2 between cysteines 150 and 162. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
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 ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35968
Residue number A
150
Residue number B
162
Peptide name
Vascular endothelial growth factor receptor 2
Ligandability
Cysteine 150 of Vascular endothelial growth factor receptor 2
Cysteine 162 of Vascular endothelial growth factor receptor 2
If this tool was useful for finding a disulphide, please cite: