ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glycine dehydrogenase (decarboxylating), mitochondrial

Intramolecular
Cysteine 210 and cysteine 291
Cysteine 442 and cysteine 444
Cysteine 444 and cysteine 490
Cysteine 184 and cysteine 1000
Cysteine 382 and cysteine 558
Cysteine 225 and cysteine 292
Cysteine 184 and cysteine 1002
Cysteine 225 and cysteine 291
Cysteine 291 and cysteine 292
A redox-regulated disulphide may form within Glycine dehydrogenase (decarboxylating), mitochondrial between cysteines 210 and 291.

Details

Redox score ?
68
PDB code
6i35
Structure name
crystal structure of human glycine decarboxylase (p-protein) bound with pyridoxyl-glycine-5'-monophosphate
Structure deposition date
2018-11-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide accession
P23378
Residue number A
210
Residue number B
291
Peptide name
Glycine dehydrogenase (decarboxylating), mitochondrial

Ligandability

Cysteine 210 of Glycine dehydrogenase (decarboxylating), 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 291 of Glycine dehydrogenase (decarboxylating), 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 Glycine dehydrogenase (decarboxylating), mitochondrial between cysteines 442 and 444.

Details

Redox score ?
67
PDB code
6i35
Structure name
crystal structure of human glycine decarboxylase (p-protein) bound with pyridoxyl-glycine-5'-monophosphate
Structure deposition date
2018-11-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
28
Peptide accession
P23378
Residue number A
442
Residue number B
444
Peptide name
Glycine dehydrogenase (decarboxylating), mitochondrial

Ligandability

Cysteine 442 of Glycine dehydrogenase (decarboxylating), 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 444 of Glycine dehydrogenase (decarboxylating), 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 Glycine dehydrogenase (decarboxylating), mitochondrial between cysteines 444 and 490. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6i33
Structure name
crystal structure of human glycine decarboxylase (p-protein)
Structure deposition date
2018-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
10
% buried
39
Peptide accession
P23378
Residue number A
444
Residue number B
490
Peptide name
Glycine dehydrogenase (decarboxylating), mitochondrial

Ligandability

Cysteine 444 of Glycine dehydrogenase (decarboxylating), 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 490 of Glycine dehydrogenase (decarboxylating), 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 Glycine dehydrogenase (decarboxylating), mitochondrial between cysteines 184 and 1000. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6i33
Structure name
crystal structure of human glycine decarboxylase (p-protein)
Structure deposition date
2018-11-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
94
Peptide accession
P23378
Residue number A
184
Residue number B
1000
Peptide name
Glycine dehydrogenase (decarboxylating), mitochondrial

Ligandability

Cysteine 184 of Glycine dehydrogenase (decarboxylating), 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 1000 of Glycine dehydrogenase (decarboxylating), 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 Glycine dehydrogenase (decarboxylating), mitochondrial between cysteines 382 and 558. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6i35
Structure name
crystal structure of human glycine decarboxylase (p-protein) bound with pyridoxyl-glycine-5'-monophosphate
Structure deposition date
2018-11-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
13
% buried
100
Peptide accession
P23378
Residue number A
382
Residue number B
558
Peptide name
Glycine dehydrogenase (decarboxylating), mitochondrial

Ligandability

Cysteine 382 of Glycine dehydrogenase (decarboxylating), 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 558 of Glycine dehydrogenase (decarboxylating), 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 Glycine dehydrogenase (decarboxylating), mitochondrial between cysteines 225 and 292. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6i35
Structure name
crystal structure of human glycine decarboxylase (p-protein) bound with pyridoxyl-glycine-5'-monophosphate
Structure deposition date
2018-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
P23378
Residue number A
225
Residue number B
292
Peptide name
Glycine dehydrogenase (decarboxylating), mitochondrial

Ligandability

Cysteine 225 of Glycine dehydrogenase (decarboxylating), 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 292 of Glycine dehydrogenase (decarboxylating), 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 Glycine dehydrogenase (decarboxylating), mitochondrial between cysteines 184 and 1002. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
6i35
Structure name
crystal structure of human glycine decarboxylase (p-protein) bound with pyridoxyl-glycine-5'-monophosphate
Structure deposition date
2018-11-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
93
Peptide accession
P23378
Residue number A
184
Residue number B
1002
Peptide name
Glycine dehydrogenase (decarboxylating), mitochondrial

Ligandability

Cysteine 184 of Glycine dehydrogenase (decarboxylating), 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 1002 of Glycine dehydrogenase (decarboxylating), 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 Glycine dehydrogenase (decarboxylating), mitochondrial between cysteines 225 and 291. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
6i35
Structure name
crystal structure of human glycine decarboxylase (p-protein) bound with pyridoxyl-glycine-5'-monophosphate
Structure deposition date
2018-11-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
14
% buried
100
Peptide accession
P23378
Residue number A
225
Residue number B
291
Peptide name
Glycine dehydrogenase (decarboxylating), mitochondrial

Ligandability

Cysteine 225 of Glycine dehydrogenase (decarboxylating), 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 291 of Glycine dehydrogenase (decarboxylating), 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 Glycine dehydrogenase (decarboxylating), mitochondrial between cysteines 291 and 292. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
6i35
Structure name
crystal structure of human glycine decarboxylase (p-protein) bound with pyridoxyl-glycine-5'-monophosphate
Structure deposition date
2018-11-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
100
Minimum pKa ?
13
% buried
100
Peptide accession
P23378
Residue number A
291
Residue number B
292
Peptide name
Glycine dehydrogenase (decarboxylating), mitochondrial

Ligandability

Cysteine 291 of Glycine dehydrogenase (decarboxylating), 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 292 of Glycine dehydrogenase (decarboxylating), 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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