ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

FLYWCH-type zinc finger-containing protein 1

Intramolecular
Cysteine 631 and cysteine 639
Cysteine 639 and cysteine 657
Cysteine 631 and cysteine 657
A redox-regulated disulphide may form within FLYWCH-type zinc finger-containing protein 1 between cysteines 631 and 639 (44 and 52 respectively in this structure).

Details

Redox score ?
83
PDB code
2rpr
Structure name
solution structure of the fifth flywch domain of flywch-type zinc finger-containing protein 1
Structure deposition date
2008-07-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
30
Peptide accession
Q4VC44
Residue number A
631
Residue number B
639
Peptide name
FLYWCH-type zinc finger-containing protein 1

Ligandability

Cysteine 631 of FLYWCH-type zinc finger-containing protein 1

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 639 of FLYWCH-type zinc finger-containing protein 1

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 FLYWCH-type zinc finger-containing protein 1 between cysteines 639 and 657 (52 and 70 respectively in this structure).

Details

Redox score ?
65
PDB code
2rpr
Structure name
solution structure of the fifth flywch domain of flywch-type zinc finger-containing protein 1
Structure deposition date
2008-07-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
41
Minimum pKa ?
8
% buried
8
Peptide accession
Q4VC44
Residue number A
639
Residue number B
657
Peptide name
FLYWCH-type zinc finger-containing protein 1

Ligandability

Cysteine 639 of FLYWCH-type zinc finger-containing protein 1

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 657 of FLYWCH-type zinc finger-containing protein 1

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 FLYWCH-type zinc finger-containing protein 1 between cysteines 631 and 657 (44 and 70 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2rpr
Structure name
solution structure of the fifth flywch domain of flywch-type zinc finger-containing protein 1
Structure deposition date
2008-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
22
Peptide accession
Q4VC44
Residue number A
631
Residue number B
657
Peptide name
FLYWCH-type zinc finger-containing protein 1

Ligandability

Cysteine 631 of FLYWCH-type zinc finger-containing protein 1

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 657 of FLYWCH-type zinc finger-containing protein 1

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: