ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein Gfi-1

Intramolecular
Cysteine 315 and cysteine 318
Cysteine 371 and cysteine 374
Cysteine 343 and cysteine 346
A redox-regulated disulphide may form within Zinc finger protein Gfi-1 between cysteines 315 and 318 (4 and 7 respectively in this structure).

Details

Redox score ?
90
PDB code
2kmk
Structure name
gfi-1 zinc fingers 3-5 complexed with dna
Structure deposition date
2009-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
6
% buried
0
Peptide accession
Q07120
Residue number A
315
Residue number B
318
Peptide name
Zinc finger protein Gfi-1

Ligandability

Cysteine 315 of Zinc finger protein Gfi-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 318 of Zinc finger protein Gfi-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 Zinc finger protein Gfi-1 between cysteines 371 and 374 (60 and 63 respectively in this structure).

Details

Redox score ?
88
PDB code
2kmk
Structure name
gfi-1 zinc fingers 3-5 complexed with dna
Structure deposition date
2009-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
0
Peptide accession
Q07120
Residue number A
371
Residue number B
374
Peptide name
Zinc finger protein Gfi-1

Ligandability

Cysteine 371 of Zinc finger protein Gfi-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 374 of Zinc finger protein Gfi-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 Zinc finger protein Gfi-1 between cysteines 343 and 346 (32 and 35 respectively in this structure).

Details

Redox score ?
86
PDB code
2kmk
Structure name
gfi-1 zinc fingers 3-5 complexed with dna
Structure deposition date
2009-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
7
% buried
0
Peptide accession
Q07120
Residue number A
343
Residue number B
346
Peptide name
Zinc finger protein Gfi-1

Ligandability

Cysteine 343 of Zinc finger protein Gfi-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 346 of Zinc finger protein Gfi-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.

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