ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Alpha-lactalbumin

Intramolecular
Cysteine 80 and cysteine 96
Cysteine 25 and cysteine 139
Cysteine 92 and cysteine 110
Cysteine 47 and cysteine 130
Cysteine 80 and cysteine 110
Cysteine 80 and cysteine 92
Cysteine 96 and cysteine 110
Cysteine 92 and cysteine 96
A redox-regulated disulphide may form within Alpha-lactalbumin between cysteines 80 and 96 (62 and 78 respectively in this structure).

Details

Redox score ?
87
PDB code
4l41
Structure name
human lactose synthase: a 2:1 complex between human alpha-lactalbumin and human beta1,4-galactosyltransferase
Structure deposition date
2013-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00709
Residue number A
80
Residue number B
96
Peptide name
Alpha-lactalbumin

Ligandability

Cysteine 80 of Alpha-lactalbumin

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 96 of Alpha-lactalbumin

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 Alpha-lactalbumin between cysteines 25 and 139 (6 and 120 respectively in this structure).

Details

Redox score ?
86
PDB code
1b9o
Structure name
human alpha-lactalbumin, low temperature form
Structure deposition date
1999-02-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00709
Residue number A
25
Residue number B
139
Peptide name
Alpha-lactalbumin

Ligandability

Cysteine 25 of Alpha-lactalbumin

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 139 of Alpha-lactalbumin

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 Alpha-lactalbumin between cysteines 92 and 110 (73 and 91 respectively in this structure).

Details

Redox score ?
84
PDB code
3b0i
Structure name
crystal structure of recombinant human alpha lactalbumin
Structure deposition date
2011-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00709
Residue number A
92
Residue number B
110
Peptide name
Alpha-lactalbumin

Ligandability

Cysteine 92 of Alpha-lactalbumin

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 110 of Alpha-lactalbumin

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 Alpha-lactalbumin between cysteines 47 and 130 (28 and 111 respectively in this structure).

Details

Redox score ?
83
PDB code
1hml
Structure name
alpha_lactalbumin possesses a distinct zinc binding site
Structure deposition date
1994-09-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00709
Residue number A
47
Residue number B
130
Peptide name
Alpha-lactalbumin

Ligandability

Cysteine 47 of Alpha-lactalbumin

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 130 of Alpha-lactalbumin

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 Alpha-lactalbumin between cysteines 80 and 110 (61 and 91 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
1hml
Structure name
alpha_lactalbumin possesses a distinct zinc binding site
Structure deposition date
1994-09-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00709
Residue number A
80
Residue number B
110
Peptide name
Alpha-lactalbumin

Ligandability

Cysteine 80 of Alpha-lactalbumin

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 110 of Alpha-lactalbumin

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 Alpha-lactalbumin between cysteines 80 and 92 (61 and 73 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
3b0i
Structure name
crystal structure of recombinant human alpha lactalbumin
Structure deposition date
2011-06-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00709
Residue number A
80
Residue number B
92
Peptide name
Alpha-lactalbumin

Ligandability

Cysteine 80 of Alpha-lactalbumin

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 92 of Alpha-lactalbumin

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 Alpha-lactalbumin between cysteines 96 and 110 (77 and 91 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
1hml
Structure name
alpha_lactalbumin possesses a distinct zinc binding site
Structure deposition date
1994-09-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00709
Residue number A
96
Residue number B
110
Peptide name
Alpha-lactalbumin

Ligandability

Cysteine 96 of Alpha-lactalbumin

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 110 of Alpha-lactalbumin

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 Alpha-lactalbumin between cysteines 92 and 96 (74 and 78 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
4l41
Structure name
human lactose synthase: a 2:1 complex between human alpha-lactalbumin and human beta1,4-galactosyltransferase
Structure deposition date
2013-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00709
Residue number A
92
Residue number B
96
Peptide name
Alpha-lactalbumin

Ligandability

Cysteine 92 of Alpha-lactalbumin

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 96 of Alpha-lactalbumin

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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