Zinc finger protein 64
Intramolecular
Cysteine 205 and cysteine 208
Cysteine 233 and cysteine 236
Cysteine 177 and cysteine 180
Cysteine 525 and cysteine 528
Cysteine 497 and cysteine 500
Cysteine 177 and cysteine 196
Cysteine 180 and cysteine 196
Cysteine 497 and cysteine 504
Cysteine 497 and cysteine 518
Cysteine 177 and cysteine 183
More...Cysteine 180 and cysteine 183
Cysteine 500 and cysteine 504
2dmd A 39 A 42
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 205 and 208 (39 and 42 respectively in this structure).
Details
Redox score ?
89
PDB code
2dmd
Structure name
solution structure of the n-terminal c2h2 type zinc-binding domain of the zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2006-04-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NPA5
Residue number A
205
Residue number B
208
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 205 of Zinc finger protein 64
Cysteine 208 of Zinc finger protein 64
2dmd A 67 A 70
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 233 and 236 (67 and 70 respectively in this structure).
Details
Redox score ?
88
PDB code
2dmd
Structure name
solution structure of the n-terminal c2h2 type zinc-binding domain of the zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2006-04-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NPA5
Residue number A
233
Residue number B
236
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 233 of Zinc finger protein 64
Cysteine 236 of Zinc finger protein 64
2dmd A 11 A 14
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 177 and 180 (11 and 14 respectively in this structure).
Details
Redox score ?
87
PDB code
2dmd
Structure name
solution structure of the n-terminal c2h2 type zinc-binding domain of the zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2006-04-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NPA5
Residue number A
177
Residue number B
180
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 177 of Zinc finger protein 64
Cysteine 180 of Zinc finger protein 64
1x5w A 40 A 43
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 525 and 528 (40 and 43 respectively in this structure).
Details
Redox score ?
86
PDB code
1x5w
Structure name
solution structure of the c2h2 type zinc-binding domain of human zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NPA5
Residue number A
525
Residue number B
528
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 525 of Zinc finger protein 64
Cysteine 528 of Zinc finger protein 64
1x5w A 12 A 15
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 497 and 500 (12 and 15 respectively in this structure).
Details
Redox score ?
84
PDB code
1x5w
Structure name
solution structure of the c2h2 type zinc-binding domain of human zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NPA5
Residue number A
497
Residue number B
500
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 497 of Zinc finger protein 64
Cysteine 500 of Zinc finger protein 64
2dmd A 11 A 30
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 177 and 196 (11 and 30 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
2dmd
Structure name
solution structure of the n-terminal c2h2 type zinc-binding domain of the zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2006-04-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
34
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NPA5
Residue number A
177
Residue number B
196
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 177 of Zinc finger protein 64
Cysteine 196 of Zinc finger protein 64
2dmd A 14 A 30
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 180 and 196 (14 and 30 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
2dmd
Structure name
solution structure of the n-terminal c2h2 type zinc-binding domain of the zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2006-04-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
26
Minimum pKa ?
9
% buried
0
Peptide accession
Q9NPA5
Residue number A
180
Residue number B
196
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 180 of Zinc finger protein 64
Cysteine 196 of Zinc finger protein 64
1x5w A 12 A 19
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 497 and 504 (12 and 19 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
1x5w
Structure name
solution structure of the c2h2 type zinc-binding domain of human zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2005-05-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NPA5
Residue number A
497
Residue number B
504
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 497 of Zinc finger protein 64
Cysteine 504 of Zinc finger protein 64
1x5w A 12 A 33
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 497 and 518 (12 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
1x5w
Structure name
solution structure of the c2h2 type zinc-binding domain of human zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2005-05-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
33
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NPA5
Residue number A
497
Residue number B
518
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 497 of Zinc finger protein 64
Cysteine 518 of Zinc finger protein 64
2dmd A 11 A 17
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 177 and 183 (11 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
2dmd
Structure name
solution structure of the n-terminal c2h2 type zinc-binding domain of the zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2006-04-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
Q9NPA5
Residue number A
177
Residue number B
183
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 177 of Zinc finger protein 64
Cysteine 183 of Zinc finger protein 64
2dmd A 14 A 17
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 180 and 183 (14 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2dmd
Structure name
solution structure of the n-terminal c2h2 type zinc-binding domain of the zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2006-04-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
30
Minimum pKa ?
9
% buried
0
Peptide accession
Q9NPA5
Residue number A
180
Residue number B
183
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 180 of Zinc finger protein 64
Cysteine 183 of Zinc finger protein 64
1x5w A 15 A 19
A redox-regulated disulphide may form within Zinc finger protein 64 between cysteines 500 and 504 (15 and 19 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1x5w
Structure name
solution structure of the c2h2 type zinc-binding domain of human zinc finger protein 64, isoforms 1 and 2
Structure deposition date
2005-05-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
0
Peptide accession
Q9NPA5
Residue number A
500
Residue number B
504
Peptide name
Zinc finger protein 64
Ligandability
Cysteine 500 of Zinc finger protein 64
Cysteine 504 of Zinc finger protein 64
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