ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transitional endoplasmic reticulum ATPase

Intramolecular
Cysteine 691 and cysteine 695
Cysteine 105 and cysteine 174
Cysteine 535 and cysteine 572
Cysteine 69 and cysteine 105
A redox-regulated disulphide may form within Transitional endoplasmic reticulum ATPase between cysteines 691 and 695. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3cf1
Structure name
structure of p97/vcp in complex with adp/adp
Structure deposition date
2008-03-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
57
Peptide accession
Q01853
Residue number A
691
Residue number B
695
Peptide name
Transitional endoplasmic reticulum ATPase

Ligandability

Cysteine 691 of Transitional endoplasmic reticulum ATPase

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 695 of Transitional endoplasmic reticulum ATPase

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 Transitional endoplasmic reticulum ATPase between cysteines 105 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7r7t
Structure name
p47-bound p97-r155h mutant with adp
Structure deposition date
2021-06-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
9
Peptide accession
P55072
Residue number A
105
Residue number B
174
Peptide name
Transitional endoplasmic reticulum ATPase

Ligandability

Cysteine 105 of Transitional endoplasmic reticulum ATPase

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 174 of Transitional endoplasmic reticulum ATPase

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 Transitional endoplasmic reticulum ATPase between cysteines 535 and 572. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7lmz
Structure name
cryo-em structure of human p97 in complex with npl4/ufd1 and ub6 (class 1)
Structure deposition date
2021-02-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
90
Peptide accession
P55072
Residue number A
535
Residue number B
572
Peptide name
Transitional endoplasmic reticulum ATPase

Ligandability

Cysteine 535 of Transitional endoplasmic reticulum ATPase

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 572 of Transitional endoplasmic reticulum ATPase

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 Transitional endoplasmic reticulum ATPase between cysteines 69 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
5ifw
Structure name
quantitative interaction mapping reveals an extended ubiquitin regulatory domain in aspl that disrupts functional p97 hexamers and induces cell death
Structure deposition date
2016-02-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
13
% buried
96
Peptide accession
P55072
Residue number A
69
Residue number B
105
Peptide name
Transitional endoplasmic reticulum ATPase

Ligandability

Cysteine 69 of Transitional endoplasmic reticulum ATPase

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 105 of Transitional endoplasmic reticulum ATPase

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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