ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Receptor-type tyrosine-protein kinase FLT3

Intramolecular
Cysteine 381 and cysteine 392
Cysteine 103 and cysteine 114
Cysteine 368 and cysteine 407
Cysteine 184 and cysteine 231
Cysteine 272 and cysteine 330
Cysteine 515 and cysteine 524
Cysteine 232 and cysteine 241
Cysteine 514 and cysteine 515
Cysteine 452 and cysteine 524
Cysteine 467 and cysteine 514
More...
Cysteine 694 and cysteine 695
Cysteine 231 and cysteine 232
Cysteine 184 and cysteine 232
Cysteine 184 and cysteine 241
Cysteine 514 and cysteine 524
Cysteine 452 and cysteine 514
Cysteine 694 and cysteine 828
Cysteine 231 and cysteine 241
Cysteine 452 and cysteine 515
A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 381 and 392.

Details

Redox score ?
90
PDB code
3qs7
Structure name
crystal structure of a human flt3 ligand-receptor ternary complex
Structure deposition date
2011-02-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P36888
Residue number A
381
Residue number B
392
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 381 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 392 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 103 and 114.

Details

Redox score ?
88
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P36888
Residue number A
103
Residue number B
114
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 103 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 114 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 368 and 407.

Details

Redox score ?
85
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P36888
Residue number A
368
Residue number B
407
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 368 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 407 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 184 and 231.

Details

Redox score ?
77
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
38
Peptide accession
P36888
Residue number A
184
Residue number B
231
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 184 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 231 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 272 and 330.

Details

Redox score ?
75
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
80
Minimum pKa ?
8
% buried
66
Peptide accession
P36888
Residue number A
272
Residue number B
330
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 272 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 330 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 515 and 524.

Details

Redox score ?
75
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
16
Peptide accession
P36888
Residue number A
515
Residue number B
524
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 515 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 524 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 232 and 241.

Details

Redox score ?
65
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
26
Peptide accession
P36888
Residue number A
232
Residue number B
241
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 232 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 241 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 514 and 515. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
22
Peptide accession
P36888
Residue number A
514
Residue number B
515
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 514 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 515 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 452 and 524. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3qs9
Structure name
crystal structure of a human flt3 ligand-receptor ternary complex
Structure deposition date
2011-02-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P36888
Residue number A
452
Residue number B
524
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 452 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 524 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 467 and 514. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
16
Peptide accession
P36888
Residue number A
467
Residue number B
514
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 467 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 514 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 694 and 695. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6jqr
Structure name
crystal structure of flt3 in complex with gilteritinib
Structure deposition date
2019-04-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
50
Peptide accession
P36888
Residue number A
694
Residue number B
695
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 694 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 695 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 231 and 232. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
nan
Peptide accession
P36888
Residue number A
231
Residue number B
232
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 231 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 232 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 184 and 232. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3qs9
Structure name
crystal structure of a human flt3 ligand-receptor ternary complex
Structure deposition date
2011-02-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P36888
Residue number A
184
Residue number B
232
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 184 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 232 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 184 and 241. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3qs7
Structure name
crystal structure of a human flt3 ligand-receptor ternary complex
Structure deposition date
2011-02-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P36888
Residue number A
184
Residue number B
241
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 184 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 241 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 514 and 524. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
nan
Peptide accession
P36888
Residue number A
514
Residue number B
524
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 514 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 524 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 452 and 514. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
20
Peptide accession
P36888
Residue number A
452
Residue number B
514
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 452 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 514 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 694 and 828. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6jqr
Structure name
crystal structure of flt3 in complex with gilteritinib
Structure deposition date
2019-04-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
91
Peptide accession
P36888
Residue number A
694
Residue number B
828
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 694 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 828 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 231 and 241. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7qdp
Structure name
crystal structure of flt3 t343i in complex with the canonical ligand fl
Structure deposition date
2021-11-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
nan
Peptide accession
P36888
Residue number A
231
Residue number B
241
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 231 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 241 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Receptor-type tyrosine-protein kinase FLT3 between cysteines 452 and 515. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3qs9
Structure name
crystal structure of a human flt3 ligand-receptor ternary complex
Structure deposition date
2011-02-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P36888
Residue number A
452
Residue number B
515
Peptide name
Receptor-type tyrosine-protein kinase FLT3

Ligandability

Cysteine 452 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 515 of Receptor-type tyrosine-protein kinase FLT3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

If this tool was useful for finding a disulphide, please cite: