ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Semaphorin-4D

Intramolecular
Cysteine 509 and cysteine 553
Cysteine 503 and cysteine 520
Cysteine 97 and cysteine 108
Cysteine 576 and cysteine 624
Cysteine 512 and cysteine 529
Cysteine 281 and cysteine 326
Cysteine 257 and cysteine 370
Cysteine 126 and cysteine 135
Cysteine 503 and cysteine 529
Cysteine 520 and cysteine 529
More...
Cysteine 503 and cysteine 512
Cysteine 512 and cysteine 520
Cysteine 509 and cysteine 512
Cysteine 512 and cysteine 553
Cysteine 135 and cysteine 156
Cysteine 126 and cysteine 156
Cysteine 509 and cysteine 529
Cysteine 529 and cysteine 553
A redox-regulated disulphide may form within Semaphorin-4D between cysteines 509 and 553.

Details

Redox score ?
87
PDB code
3ol2
Structure name
receptor-ligand structure of human semaphorin 4d with plexin b1
Structure deposition date
2010-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
509
Residue number B
553
Peptide name
Semaphorin-4D

Ligandability

Cysteine 509 of Semaphorin-4D

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 553 of Semaphorin-4D

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 Semaphorin-4D between cysteines 503 and 520.

Details

Redox score ?
83
PDB code
3ol2
Structure name
receptor-ligand structure of human semaphorin 4d with plexin b1
Structure deposition date
2010-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
503
Residue number B
520
Peptide name
Semaphorin-4D

Ligandability

Cysteine 503 of Semaphorin-4D

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 520 of Semaphorin-4D

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 Semaphorin-4D between cysteines 97 and 108.

Details

Redox score ?
83
PDB code
3ol2
Structure name
receptor-ligand structure of human semaphorin 4d with plexin b1
Structure deposition date
2010-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
97
Residue number B
108
Peptide name
Semaphorin-4D

Ligandability

Cysteine 97 of Semaphorin-4D

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 108 of Semaphorin-4D

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 Semaphorin-4D between cysteines 576 and 624 (555 and 603 respectively in this structure).

Details

Redox score ?
82
PDB code
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
576
Residue number B
624
Peptide name
Semaphorin-4D

Ligandability

Cysteine 576 of Semaphorin-4D

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 624 of Semaphorin-4D

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 Semaphorin-4D between cysteines 512 and 529 (491 and 508 respectively in this structure).

Details

Redox score ?
82
PDB code
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
512
Residue number B
529
Peptide name
Semaphorin-4D

Ligandability

Cysteine 512 of Semaphorin-4D

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 529 of Semaphorin-4D

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 Semaphorin-4D between cysteines 281 and 326 (260 and 305 respectively in this structure).

Details

Redox score ?
80
PDB code
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
281
Residue number B
326
Peptide name
Semaphorin-4D

Ligandability

Cysteine 281 of Semaphorin-4D

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 326 of Semaphorin-4D

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 Semaphorin-4D between cysteines 257 and 370 (236 and 349 respectively in this structure).

Details

Redox score ?
79
PDB code
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
257
Residue number B
370
Peptide name
Semaphorin-4D

Ligandability

Cysteine 257 of Semaphorin-4D

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 370 of Semaphorin-4D

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 Semaphorin-4D between cysteines 126 and 135.

Details

Redox score ?
78
PDB code
3ol2
Structure name
receptor-ligand structure of human semaphorin 4d with plexin b1
Structure deposition date
2010-08-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
126
Residue number B
135
Peptide name
Semaphorin-4D

Ligandability

Cysteine 126 of Semaphorin-4D

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 135 of Semaphorin-4D

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 Semaphorin-4D between cysteines 503 and 529 (482 and 508 respectively in this structure).

Details

Redox score ?
69
PDB code
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
503
Residue number B
529
Peptide name
Semaphorin-4D

Ligandability

Cysteine 503 of Semaphorin-4D

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 529 of Semaphorin-4D

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 Semaphorin-4D between cysteines 520 and 529 (499 and 508 respectively in this structure).

Details

Redox score ?
68
PDB code
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
520
Residue number B
529
Peptide name
Semaphorin-4D

Ligandability

Cysteine 520 of Semaphorin-4D

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 529 of Semaphorin-4D

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 Semaphorin-4D between cysteines 503 and 512 (482 and 491 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
503
Residue number B
512
Peptide name
Semaphorin-4D

Ligandability

Cysteine 503 of Semaphorin-4D

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 Semaphorin-4D

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 Semaphorin-4D between cysteines 512 and 520. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3ol2
Structure name
receptor-ligand structure of human semaphorin 4d with plexin b1
Structure deposition date
2010-08-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
512
Residue number B
520
Peptide name
Semaphorin-4D

Ligandability

Cysteine 512 of Semaphorin-4D

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 520 of Semaphorin-4D

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 Semaphorin-4D between cysteines 509 and 512 (488 and 491 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
509
Residue number B
512
Peptide name
Semaphorin-4D

Ligandability

Cysteine 509 of Semaphorin-4D

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 Semaphorin-4D

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 Semaphorin-4D between cysteines 512 and 553. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3ol2
Structure name
receptor-ligand structure of human semaphorin 4d with plexin b1
Structure deposition date
2010-08-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
512
Residue number B
553
Peptide name
Semaphorin-4D

Ligandability

Cysteine 512 of Semaphorin-4D

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 553 of Semaphorin-4D

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 Semaphorin-4D between cysteines 135 and 156. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3ol2
Structure name
receptor-ligand structure of human semaphorin 4d with plexin b1
Structure deposition date
2010-08-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
nan
Peptide accession
Q92854
Residue number A
135
Residue number B
156
Peptide name
Semaphorin-4D

Ligandability

Cysteine 135 of Semaphorin-4D

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 156 of Semaphorin-4D

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 Semaphorin-4D between cysteines 126 and 156 (105 and 135 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
nan
Peptide accession
Q92854
Residue number A
126
Residue number B
156
Peptide name
Semaphorin-4D

Ligandability

Cysteine 126 of Semaphorin-4D

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 156 of Semaphorin-4D

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 Semaphorin-4D between cysteines 509 and 529 (488 and 508 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
1olz
Structure name
the ligand-binding face of the semaphorins revealed by the high resolution crystal structure of sema4d
Structure deposition date
2003-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
509
Residue number B
529
Peptide name
Semaphorin-4D

Ligandability

Cysteine 509 of Semaphorin-4D

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 529 of Semaphorin-4D

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 Semaphorin-4D between cysteines 529 and 553. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3ol2
Structure name
receptor-ligand structure of human semaphorin 4d with plexin b1
Structure deposition date
2010-08-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92854
Residue number A
529
Residue number B
553
Peptide name
Semaphorin-4D

Ligandability

Cysteine 529 of Semaphorin-4D

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 553 of Semaphorin-4D

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: