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Deformed epidermal autoregulatory factor 1 homolog

Intramolecular
Cysteine 504 and cysteine 528
Cysteine 504 and cysteine 524
Cysteine 504 and cysteine 507
Cysteine 515 and cysteine 540 L
Cysteine 518 and cysteine 540
Cysteine 515 and cysteine 518 L
Cysteine 524 and cysteine 528
Cysteine 507 and cysteine 528
Cysteine 507 and cysteine 524
Cysteine 541 and cysteine 112
More...
Cysteine 525 and cysteine 137
Cysteine 228 and cysteine 541
Cysteine 228 and cysteine 112
Cysteine 484 and cysteine 137
A redox-regulated disulphide may form within Deformed epidermal autoregulatory factor 1 homolog between cysteines 504 and 528.

Details

Redox score ?
90
PDB code
2jw6
Structure name
solution structure of the deaf1 mynd domain
Structure deposition date
2007-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
0
Peptide accession
O75398
Residue number A
504
Residue number B
528
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 504 of Deformed epidermal autoregulatory factor 1 homolog

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 528 of Deformed epidermal autoregulatory factor 1 homolog

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 Deformed epidermal autoregulatory factor 1 homolog between cysteines 504 and 524.

Details

Redox score ?
88
PDB code
2jw6
Structure name
solution structure of the deaf1 mynd domain
Structure deposition date
2007-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
0
Peptide accession
O75398
Residue number A
504
Residue number B
524
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 504 of Deformed epidermal autoregulatory factor 1 homolog

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 524 of Deformed epidermal autoregulatory factor 1 homolog

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 Deformed epidermal autoregulatory factor 1 homolog between cysteines 504 and 507.

Details

Redox score ?
88
PDB code
2jw6
Structure name
solution structure of the deaf1 mynd domain
Structure deposition date
2007-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
0
Peptide accession
O75398
Residue number A
504
Residue number B
507
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 504 of Deformed epidermal autoregulatory factor 1 homolog

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 507 of Deformed epidermal autoregulatory factor 1 homolog

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 Deformed epidermal autoregulatory factor 1 homolog between cysteines 515 and 540.

Details

Redox score ?
86
PDB code
4a24
Structure name
structural and functional analysis of the deaf-1 and bs69 mynd domains
Structure deposition date
2011-09-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
1
Peptide accession
O75398
Residue number A
515
Residue number B
540
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 515 of Deformed epidermal autoregulatory factor 1 homolog

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 540 of Deformed epidermal autoregulatory factor 1 homolog

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 Deformed epidermal autoregulatory factor 1 homolog between cysteines 518 and 540.

Details

Redox score ?
85
PDB code
2jw6
Structure name
solution structure of the deaf1 mynd domain
Structure deposition date
2007-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
0
Peptide accession
O75398
Residue number A
518
Residue number B
540
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 518 of Deformed epidermal autoregulatory factor 1 homolog

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 540 of Deformed epidermal autoregulatory factor 1 homolog

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 Deformed epidermal autoregulatory factor 1 homolog between cysteines 515 and 518.

Details

Redox score ?
83
PDB code
2jw6
Structure name
solution structure of the deaf1 mynd domain
Structure deposition date
2007-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
2
Peptide accession
O75398
Residue number A
515
Residue number B
518
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 515 of Deformed epidermal autoregulatory factor 1 homolog

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 518 of Deformed epidermal autoregulatory factor 1 homolog

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 Deformed epidermal autoregulatory factor 1 homolog between cysteines 524 and 528.

Details

Redox score ?
82
PDB code
2jw6
Structure name
solution structure of the deaf1 mynd domain
Structure deposition date
2007-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
0
Peptide accession
O75398
Residue number A
524
Residue number B
528
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 524 of Deformed epidermal autoregulatory factor 1 homolog

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 528 of Deformed epidermal autoregulatory factor 1 homolog

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 Deformed epidermal autoregulatory factor 1 homolog between cysteines 507 and 528.

Details

Redox score ?
77
PDB code
2jw6
Structure name
solution structure of the deaf1 mynd domain
Structure deposition date
2007-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
10
% buried
0
Peptide accession
O75398
Residue number A
507
Residue number B
528
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 507 of Deformed epidermal autoregulatory factor 1 homolog

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 528 of Deformed epidermal autoregulatory factor 1 homolog

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 Deformed epidermal autoregulatory factor 1 homolog between cysteines 507 and 524.

Details

Redox score ?
76
PDB code
4a24
Structure name
structural and functional analysis of the deaf-1 and bs69 mynd domains
Structure deposition date
2011-09-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
0
Peptide accession
O75398
Residue number A
507
Residue number B
524
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 507 of Deformed epidermal autoregulatory factor 1 homolog

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 524 of Deformed epidermal autoregulatory factor 1 homolog

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 Deformed epidermal autoregulatory factor 1 homolog between cysteines 541 and 112 (90 and 112 respectively in this structure).

Details

Redox score ?
nan
PDB code
2mbv
Structure name
lmo4-lim2 in complex with deaf1 (404-418)
Structure deposition date
2013-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
18
Peptide accession
Q9Z1T5
Residue number A
541
Residue number B
112
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 541 of Deformed epidermal autoregulatory factor 1 homolog

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 112 of Deformed epidermal autoregulatory factor 1 homolog

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 112 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Deformed epidermal autoregulatory factor 1 homolog between cysteines 525 and 137 (115 and 137 respectively in this structure).

Details

Redox score ?
nan
PDB code
2mbv
Structure name
lmo4-lim2 in complex with deaf1 (404-418)
Structure deposition date
2013-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
10
Peptide accession
Q9Z1T5
Residue number A
525
Residue number B
137
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 525 of Deformed epidermal autoregulatory factor 1 homolog

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 137 of Deformed epidermal autoregulatory factor 1 homolog

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 137 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Deformed epidermal autoregulatory factor 1 homolog between cysteines 228 and 541 (87 and 90 respectively in this structure).

Details

Redox score ?
nan
PDB code
2mbv
Structure name
lmo4-lim2 in complex with deaf1 (404-418)
Structure deposition date
2013-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
22
Peptide accession
Q9Z1T5
Residue number A
228
Residue number B
541
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 228 of Deformed epidermal autoregulatory factor 1 homolog

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 541 of Deformed epidermal autoregulatory factor 1 homolog

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.

Uncertain whether structure cysteine 87 has been assigned to correct residue.
A redox-regulated disulphide may form within Deformed epidermal autoregulatory factor 1 homolog between cysteines 228 and 112 (87 and 112 respectively in this structure).

Details

Redox score ?
nan
PDB code
2mbv
Structure name
lmo4-lim2 in complex with deaf1 (404-418)
Structure deposition date
2013-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
31
Peptide accession
Q9Z1T5
Residue number A
228
Residue number B
112
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 228 of Deformed epidermal autoregulatory factor 1 homolog

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 112 of Deformed epidermal autoregulatory factor 1 homolog

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.

Uncertain whether structure cysteine 87 has been assigned to correct residue.
Cysteine 112 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Deformed epidermal autoregulatory factor 1 homolog between cysteines 484 and 137 (118 and 137 respectively in this structure).

Details

Redox score ?
nan
PDB code
2mbv
Structure name
lmo4-lim2 in complex with deaf1 (404-418)
Structure deposition date
2013-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
4
Peptide accession
Q9Z1T5
Residue number A
484
Residue number B
137
Peptide name
Deformed epidermal autoregulatory factor 1 homolog

Ligandability

Cysteine 484 of Deformed epidermal autoregulatory factor 1 homolog

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 137 of Deformed epidermal autoregulatory factor 1 homolog

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 137 in protein B could not be asigned to a Uniprot residue.
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