ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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NEDD8-conjugating enzyme Ubc12

Intramolecular
Cysteine 47 and cysteine 65
Cysteine 95 and cysteine 181 L
Cysteine 65 and cysteine 181
A redox-regulated disulphide may form within NEDD8-conjugating enzyme Ubc12 between cysteines 47 and 65. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2nvu
Structure name
structure of appbp1-uba3~nedd8-nedd8-mgatp-ubc12(c111a), a trapped ubiquitin-like protein activation complex
Structure deposition date
2006-11-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
44
Peptide accession
P61081
Residue number A
47
Residue number B
65
Peptide name
NEDD8-conjugating enzyme Ubc12

Ligandability

Cysteine 47 of NEDD8-conjugating enzyme Ubc12

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 65 of NEDD8-conjugating enzyme Ubc12

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 NEDD8-conjugating enzyme Ubc12 between cysteines 95 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2nvu
Structure name
structure of appbp1-uba3~nedd8-nedd8-mgatp-ubc12(c111a), a trapped ubiquitin-like protein activation complex
Structure deposition date
2006-11-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
71
Peptide accession
P61081
Residue number A
95
Residue number B
181
Peptide name
NEDD8-conjugating enzyme Ubc12

Ligandability

Cysteine 95 of NEDD8-conjugating enzyme Ubc12

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 181 of NEDD8-conjugating enzyme Ubc12

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 NEDD8-conjugating enzyme Ubc12 between cysteines 65 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2nvu
Structure name
structure of appbp1-uba3~nedd8-nedd8-mgatp-ubc12(c111a), a trapped ubiquitin-like protein activation complex
Structure deposition date
2006-11-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
42
Peptide accession
P61081
Residue number A
65
Residue number B
181
Peptide name
NEDD8-conjugating enzyme Ubc12

Ligandability

Cysteine 65 of NEDD8-conjugating enzyme Ubc12

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 181 of NEDD8-conjugating enzyme Ubc12

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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