ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Beta-lactoglobulin-1/B

Intramolecular
Cysteine 84 and cysteine 178 L
Cysteine 122 and cysteine 135
Cysteine 124 and cysteine 137
Cysteine 100 and cysteine 103
Cysteine 122 and cysteine 137
Cysteine 154 and cysteine 523
A redox-regulated disulphide may form within Beta-lactoglobulin-1/B between cysteines 84 and 178 (66 and 160 respectively in this structure).

Details

Redox score ?
87
PDB code
4nlj
Structure name
crystal structure of sheep beta-lactoglobulin (space group p1)
Structure deposition date
2013-11-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P67976
Residue number A
84
Residue number B
178
Peptide name
Beta-lactoglobulin-1/B

Ligandability

Cysteine 84 of Beta-lactoglobulin-1/B

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 178 of Beta-lactoglobulin-1/B

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.

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.

A redox-regulated disulphide may form within Beta-lactoglobulin between cysteines 122 and 135 (106 and 119 respectively in this structure).

Details

Redox score ?
79
PDB code
1b0o
Structure name
bovine beta-lactoglobulin complexed with palmitate, lattice z
Structure deposition date
1998-11-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02754
Residue number A
122
Residue number B
135
Peptide name
Beta-lactoglobulin

Ligandability

Cysteine 122 of Beta-lactoglobulin

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 135 of Beta-lactoglobulin

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 Beta-lactoglobulin-1A/1C between cysteines 124 and 137 (106 and 119 respectively in this structure).

Details

Redox score ?
79
PDB code
1exs
Structure name
structure of porcine beta-lactoglobulin
Structure deposition date
2000-05-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04119
Residue number A
124
Residue number B
137
Peptide name
Beta-lactoglobulin-1A/1C

Ligandability

Cysteine 124 of Beta-lactoglobulin-1A/1C

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 Beta-lactoglobulin-1A/1C

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 Serine beta-lactamase-like protein LACTB, mitochondrial between cysteines 100 and 103. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7ulw
Structure name
cryoem structure of human lactb filament
Structure deposition date
2022-04-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
31
Minimum pKa ?
8
% buried
0
Peptide accession
P83111
Residue number A
100
Residue number B
103
Peptide name
Serine beta-lactamase-like protein LACTB, mitochondrial

Ligandability

Cysteine 100 of Serine beta-lactamase-like protein LACTB, mitochondrial

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 103 of Serine beta-lactamase-like protein LACTB, mitochondrial

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 Beta-lactoglobulin between cysteines 122 and 137 (106 and 121 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1cj5
Structure name
bovine beta-lactoglobulin a
Structure deposition date
1999-04-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
99
Peptide accession
P02754
Residue number A
122
Residue number B
137
Peptide name
Beta-lactoglobulin

Ligandability

Cysteine 122 of Beta-lactoglobulin

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 Beta-lactoglobulin

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 Serine beta-lactamase-like protein LACTB, mitochondrial between cysteines 154 and 523. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
7v1z
Structure name
human serine beta-lactamase-like protein lactb
Structure deposition date
2021-08-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
92
Peptide accession
P83111
Residue number A
154
Residue number B
523
Peptide name
Serine beta-lactamase-like protein LACTB, mitochondrial

Ligandability

Cysteine 154 of Serine beta-lactamase-like protein LACTB, mitochondrial

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 523 of Serine beta-lactamase-like protein LACTB, mitochondrial

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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