ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein ZIC 3

Intramolecular
Cysteine 360 and cysteine 365
Cysteine 330 and cysteine 335
Cysteine 297 and cysteine 302
Cysteine 253 and cysteine 268
Cysteine 253 and cysteine 297
A redox-regulated disulphide may form within Zinc finger protein ZIC 3 between cysteines 360 and 365 (123 and 128 respectively in this structure).

Details

Redox score ?
84
PDB code
2rpc
Structure name
solution structure of the tandem zf-c2h2 domains from the human zinc finger protein zic 3
Structure deposition date
2008-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
O60481
Residue number A
360
Residue number B
365
Peptide name
Zinc finger protein ZIC 3

Ligandability

Cysteine 360 of Zinc finger protein ZIC 3

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 365 of Zinc finger protein ZIC 3

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 ZIC 3 between cysteines 330 and 335 (93 and 98 respectively in this structure).

Details

Redox score ?
84
PDB code
2rpc
Structure name
solution structure of the tandem zf-c2h2 domains from the human zinc finger protein zic 3
Structure deposition date
2008-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
O60481
Residue number A
330
Residue number B
335
Peptide name
Zinc finger protein ZIC 3

Ligandability

Cysteine 330 of Zinc finger protein ZIC 3

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 335 of Zinc finger protein ZIC 3

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 ZIC 3 between cysteines 297 and 302 (60 and 65 respectively in this structure).

Details

Redox score ?
81
PDB code
2rpc
Structure name
solution structure of the tandem zf-c2h2 domains from the human zinc finger protein zic 3
Structure deposition date
2008-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
48
Peptide accession
O60481
Residue number A
297
Residue number B
302
Peptide name
Zinc finger protein ZIC 3

Ligandability

Cysteine 297 of Zinc finger protein ZIC 3

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 302 of Zinc finger protein ZIC 3

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 ZIC 3 between cysteines 253 and 268 (16 and 31 respectively in this structure).

Details

Redox score ?
80
PDB code
2rpc
Structure name
solution structure of the tandem zf-c2h2 domains from the human zinc finger protein zic 3
Structure deposition date
2008-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
38
Peptide accession
O60481
Residue number A
253
Residue number B
268
Peptide name
Zinc finger protein ZIC 3

Ligandability

Cysteine 253 of Zinc finger protein ZIC 3

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 268 of Zinc finger protein ZIC 3

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 ZIC 3 between cysteines 253 and 297 (16 and 60 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2rpc
Structure name
solution structure of the tandem zf-c2h2 domains from the human zinc finger protein zic 3
Structure deposition date
2008-05-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
56
Peptide accession
O60481
Residue number A
253
Residue number B
297
Peptide name
Zinc finger protein ZIC 3

Ligandability

Cysteine 253 of Zinc finger protein ZIC 3

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 297 of Zinc finger protein ZIC 3

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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