ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Protein zwilch homolog

Intramolecular
Cysteine 149 and cysteine 172
Cysteine 477 and cysteine 495
Cysteine 140 and cysteine 149
A redox-regulated disulphide may form within Protein zwilch homolog between cysteines 149 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3if8
Structure name
crystal structure of zwilch, a member of the rzz kinetochore complex
Structure deposition date
2009-07-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
82
Peptide accession
Q9H900
Residue number A
149
Residue number B
172
Peptide name
Protein zwilch homolog

Ligandability

Cysteine 149 of Protein zwilch homolog

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 172 of Protein zwilch homolog

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 Protein zwilch homolog between cysteines 477 and 495. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3if8
Structure name
crystal structure of zwilch, a member of the rzz kinetochore complex
Structure deposition date
2009-07-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
90
Peptide accession
Q9H900
Residue number A
477
Residue number B
495
Peptide name
Protein zwilch homolog

Ligandability

Cysteine 477 of Protein zwilch homolog

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 495 of Protein zwilch homolog

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 Protein zwilch homolog between cysteines 140 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3if8
Structure name
crystal structure of zwilch, a member of the rzz kinetochore complex
Structure deposition date
2009-07-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
86
Peptide accession
Q9H900
Residue number A
140
Residue number B
149
Peptide name
Protein zwilch homolog

Ligandability

Cysteine 140 of Protein zwilch homolog

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 149 of Protein zwilch homolog

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: