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Slit homolog 2 protein

Intramolecular
Cysteine 727 and cysteine 733
Cysteine 865 and cysteine 907
Cysteine 436 and cysteine 478
Cysteine 273 and cysteine 279
Cysteine 506 and cysteine 512 L
Cysteine 277 and cysteine 286
Cysteine 731 and cysteine 740
Cysteine 510 and cysteine 519 L
Cysteine 670 and cysteine 712
Cysteine 434 and cysteine 457
More...
Cysteine 863 and cysteine 886
Cysteine 668 and cysteine 691
Cysteine 727 and cysteine 731
Cysteine 277 and cysteine 279
Cysteine 731 and cysteine 733
Cysteine 506 and cysteine 510
Cysteine 273 and cysteine 277
Cysteine 510 and cysteine 512 L
Cysteine 279 and cysteine 286
Cysteine 727 and cysteine 740
Cysteine 512 and cysteine 519 L
Cysteine 733 and cysteine 740
Cysteine 506 and cysteine 519 L
Cysteine 273 and cysteine 286
A redox-regulated disulphide may form within Slit homolog 2 protein between cysteines 727 and 733.

Details

Redox score ?
91
PDB code
2wfh
Structure name
the human slit 2 dimerization domain d4
Structure deposition date
2009-04-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
727
Residue number B
733
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 727 of Slit homolog 2 protein

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 733 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 865 and 907.

Details

Redox score ?
89
PDB code
2wfh
Structure name
the human slit 2 dimerization domain d4
Structure deposition date
2009-04-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
865
Residue number B
907
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 865 of Slit homolog 2 protein

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 907 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 436 and 478.

Details

Redox score ?
89
PDB code
2v9s
Structure name
second lrr domain of human slit2
Structure deposition date
2007-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
436
Residue number B
478
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 436 of Slit homolog 2 protein

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 478 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 273 and 279.

Details

Redox score ?
88
PDB code
2v9s
Structure name
second lrr domain of human slit2
Structure deposition date
2007-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
273
Residue number B
279
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 273 of Slit homolog 2 protein

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 279 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 506 and 512.

Details

Redox score ?
88
PDB code
2v70
Structure name
third lrr domain of human slit2
Structure deposition date
2007-07-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
506
Residue number B
512
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 506 of Slit homolog 2 protein

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 512 of Slit homolog 2 protein

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Slit homolog 2 protein between cysteines 277 and 286.

Details

Redox score ?
86
PDB code
2v9s
Structure name
second lrr domain of human slit2
Structure deposition date
2007-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
277
Residue number B
286
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 277 of Slit homolog 2 protein

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 286 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 731 and 740.

Details

Redox score ?
86
PDB code
2wfh
Structure name
the human slit 2 dimerization domain d4
Structure deposition date
2009-04-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
731
Residue number B
740
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 731 of Slit homolog 2 protein

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 740 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 510 and 519.

Details

Redox score ?
85
PDB code
2v70
Structure name
third lrr domain of human slit2
Structure deposition date
2007-07-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
510
Residue number B
519
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 510 of Slit homolog 2 protein

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 519 of Slit homolog 2 protein

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Slit homolog 2 protein between cysteines 670 and 712.

Details

Redox score ?
85
PDB code
2v70
Structure name
third lrr domain of human slit2
Structure deposition date
2007-07-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
670
Residue number B
712
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 670 of Slit homolog 2 protein

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 712 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 434 and 457.

Details

Redox score ?
84
PDB code
2v9s
Structure name
second lrr domain of human slit2
Structure deposition date
2007-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
434
Residue number B
457
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 434 of Slit homolog 2 protein

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 457 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 863 and 886.

Details

Redox score ?
83
PDB code
2wfh
Structure name
the human slit 2 dimerization domain d4
Structure deposition date
2009-04-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
863
Residue number B
886
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 863 of Slit homolog 2 protein

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 886 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 668 and 691.

Details

Redox score ?
82
PDB code
2v70
Structure name
third lrr domain of human slit2
Structure deposition date
2007-07-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
668
Residue number B
691
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 668 of Slit homolog 2 protein

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 691 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 727 and 731.

Details

Redox score ?
69
PDB code
2wfh
Structure name
the human slit 2 dimerization domain d4
Structure deposition date
2009-04-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
727
Residue number B
731
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 727 of Slit homolog 2 protein

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 731 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 277 and 279.

Details

Redox score ?
67
PDB code
2v9s
Structure name
second lrr domain of human slit2
Structure deposition date
2007-08-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
277
Residue number B
279
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 277 of Slit homolog 2 protein

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 279 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 731 and 733.

Details

Redox score ?
67
PDB code
2wfh
Structure name
the human slit 2 dimerization domain d4
Structure deposition date
2009-04-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
731
Residue number B
733
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 731 of Slit homolog 2 protein

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 733 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 506 and 510.

Details

Redox score ?
66
PDB code
2v70
Structure name
third lrr domain of human slit2
Structure deposition date
2007-07-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
506
Residue number B
510
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 506 of Slit homolog 2 protein

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 510 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 273 and 277.

Details

Redox score ?
65
PDB code
2v9s
Structure name
second lrr domain of human slit2
Structure deposition date
2007-08-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
273
Residue number B
277
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 273 of Slit homolog 2 protein

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 277 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 510 and 512.

Details

Redox score ?
65
PDB code
2v70
Structure name
third lrr domain of human slit2
Structure deposition date
2007-07-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
510
Residue number B
512
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 510 of Slit homolog 2 protein

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 512 of Slit homolog 2 protein

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Slit homolog 2 protein between cysteines 279 and 286.

Details

Redox score ?
62
PDB code
2v9s
Structure name
second lrr domain of human slit2
Structure deposition date
2007-08-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
279
Residue number B
286
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 279 of Slit homolog 2 protein

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 286 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 727 and 740. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
2wfh
Structure name
the human slit 2 dimerization domain d4
Structure deposition date
2009-04-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
727
Residue number B
740
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 727 of Slit homolog 2 protein

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 740 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 512 and 519. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2v70
Structure name
third lrr domain of human slit2
Structure deposition date
2007-07-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
512
Residue number B
519
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 512 of Slit homolog 2 protein

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 519 of Slit homolog 2 protein

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Slit homolog 2 protein between cysteines 733 and 740. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2wfh
Structure name
the human slit 2 dimerization domain d4
Structure deposition date
2009-04-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
733
Residue number B
740
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 733 of Slit homolog 2 protein

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 740 of Slit homolog 2 protein

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 Slit homolog 2 protein between cysteines 506 and 519. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
2v70
Structure name
third lrr domain of human slit2
Structure deposition date
2007-07-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
506
Residue number B
519
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 506 of Slit homolog 2 protein

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 519 of Slit homolog 2 protein

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Slit homolog 2 protein between cysteines 273 and 286. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2v9t
Structure name
complex between the second lrr domain of slit2 and the first ig domain from robo1
Structure deposition date
2007-08-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
O94813
Residue number A
273
Residue number B
286
Peptide name
Slit homolog 2 protein

Ligandability

Cysteine 273 of Slit homolog 2 protein

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 286 of Slit homolog 2 protein

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.

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