ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Endoglin

Intramolecular
Cysteine 350 and cysteine 382
Cysteine 242 and cysteine 330
Cysteine 394 and cysteine 412
Cysteine 493 and cysteine 549
Cysteine 53 and cysteine 182
Cysteine 30 and cysteine 207
Cysteine 363 and cysteine 442
A redox-regulated disulphide may form within Endoglin between cysteines 350 and 382 (750 and 782 respectively in this structure).

Details

Redox score ?
90
PDB code
5hzv
Structure name
crystal structure of the zona pellucida module of human endoglin/cd105
Structure deposition date
2016-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17813
Residue number A
350
Residue number B
382
Peptide name
Endoglin

Ligandability

Cysteine 350 of Endoglin

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 382 of Endoglin

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 Endoglin between cysteines 242 and 330 (642 and 730 respectively in this structure).

Details

Redox score ?
89
PDB code
5hzw
Structure name
crystal structure of the orphan region of human endoglin/cd105 in complex with bmp9
Structure deposition date
2016-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17813
Residue number A
242
Residue number B
330
Peptide name
Endoglin

Ligandability

Cysteine 242 of Endoglin

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 Endoglin

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 Endoglin between cysteines 394 and 412 (794 and 812 respectively in this structure).

Details

Redox score ?
86
PDB code
5hzv
Structure name
crystal structure of the zona pellucida module of human endoglin/cd105
Structure deposition date
2016-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17813
Residue number A
394
Residue number B
412
Peptide name
Endoglin

Ligandability

Cysteine 394 of Endoglin

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 412 of Endoglin

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 Endoglin between cysteines 493 and 549 (893 and 949 respectively in this structure).

Details

Redox score ?
85
PDB code
5hzv
Structure name
crystal structure of the zona pellucida module of human endoglin/cd105
Structure deposition date
2016-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17813
Residue number A
493
Residue number B
549
Peptide name
Endoglin

Ligandability

Cysteine 493 of Endoglin

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 549 of Endoglin

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 Endoglin between cysteines 53 and 182 (453 and 582 respectively in this structure).

Details

Redox score ?
83
PDB code
5hzw
Structure name
crystal structure of the orphan region of human endoglin/cd105 in complex with bmp9
Structure deposition date
2016-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17813
Residue number A
53
Residue number B
182
Peptide name
Endoglin

Ligandability

Cysteine 53 of Endoglin

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 182 of Endoglin

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 Endoglin between cysteines 30 and 207 (430 and 607 respectively in this structure).

Details

Redox score ?
81
PDB code
5hzw
Structure name
crystal structure of the orphan region of human endoglin/cd105 in complex with bmp9
Structure deposition date
2016-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17813
Residue number A
30
Residue number B
207
Peptide name
Endoglin

Ligandability

Cysteine 30 of Endoglin

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 207 of Endoglin

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 Endoglin between cysteines 363 and 442 (763 and 842 respectively in this structure).

Details

Redox score ?
80
PDB code
5hzv
Structure name
crystal structure of the zona pellucida module of human endoglin/cd105
Structure deposition date
2016-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17813
Residue number A
363
Residue number B
442
Peptide name
Endoglin

Ligandability

Cysteine 363 of Endoglin

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 442 of Endoglin

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: