a tool for identifying drug-targetable redox-active disulphides

Zinc finger protein GLI1

Intramolecular

Cysteine 303 and cysteine 308

Cysteine 364 and cysteine 369

Cysteine 333 and cysteine 338

Cysteine 237 and cysteine 242

Cysteine 270 and cysteine 275

Cysteine 237 and cysteine 270

A redox-regulated disulphide may form within Zinc finger protein GLI1 between cysteines 303 and 308 (172 and 177 respectively in this structure).

Details

Redox score ?

90

PDB code

Structure name

five-finger gli/dna complex

Structure deposition date

1993-11-09

Thiol separation (Å)

3

Half-sphere exposure sum ?

38

Minimum pK_a ?

7

% buried

0

Peptide accession

Residue number A

303

Residue number B

308

Peptide name

Zinc finger protein GLI1

Ligandability

Cysteine 303 of Zinc finger protein GLI1

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 308 of Zinc finger protein GLI1

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 GLI1 between cysteines 364 and 369 (233 and 238 respectively in this structure).

Details

Redox score ?

86

PDB code

Structure name

five-finger gli/dna complex

Structure deposition date

1993-11-09

Thiol separation (Å)

4

Half-sphere exposure sum ?

40

Minimum pK_a ?

8

% buried

0

Peptide accession

Residue number A

364

Residue number B

369

Peptide name

Zinc finger protein GLI1

Ligandability

Cysteine 364 of Zinc finger protein GLI1

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 369 of Zinc finger protein GLI1

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 GLI1 between cysteines 333 and 338 (202 and 207 respectively in this structure).

Details

Redox score ?

83

PDB code

Structure name

five-finger gli/dna complex

Structure deposition date

1993-11-09

Thiol separation (Å)

4

Half-sphere exposure sum ?

43

Minimum pK_a ?

8

% buried

4

Peptide accession

Residue number A

333

Residue number B

338

Peptide name

Zinc finger protein GLI1

Ligandability

Cysteine 333 of Zinc finger protein GLI1

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 338 of Zinc finger protein GLI1

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 GLI1 between cysteines 237 and 242.

Details

Redox score ?

83

PDB code

Structure name

crystal structure of zinc finger motif 1 and 2 of gli1 dna binding region

Structure deposition date

2021-12-17

Thiol separation (Å)

4

Half-sphere exposure sum ?

50

Minimum pK_a ?

8

% buried

30

Peptide accession

Residue number A

237

Residue number B

242

Peptide name

Zinc finger protein GLI1

Ligandability

Cysteine 237 of Zinc finger protein GLI1

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 242 of Zinc finger protein GLI1

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 GLI1 between cysteines 270 and 275.

Details

Redox score ?

80

PDB code

Structure name

crystal structure of zinc finger motif 1 and 2 of gli1 dna binding region

Structure deposition date

2021-12-17

Thiol separation (Å)

4

Half-sphere exposure sum ?

57

Minimum pK_a ?

8

% buried

39

Peptide accession

Residue number A

270

Residue number B

275

Peptide name

Zinc finger protein GLI1

Ligandability

Cysteine 270 of Zinc finger protein GLI1

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 275 of Zinc finger protein GLI1

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 GLI1 between cysteines 237 and 270 (106 and 139 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

42

PDB code

Structure name

five-finger gli/dna complex

Structure deposition date

1993-11-09

Thiol separation (Å)

9

Half-sphere exposure sum ?

68

Minimum pK_a ?

10

% buried

48

Peptide accession

Residue number A

237

Residue number B

270

Peptide name

Zinc finger protein GLI1

Ligandability

Cysteine 237 of Zinc finger protein GLI1

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 270 of Zinc finger protein GLI1

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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