ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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CLIP-associating protein 1

Intramolecular
Cysteine 453 and cysteine 464 L
Cysteine 453 and cysteine 509 L
Cysteine 464 and cysteine 509
A redox-regulated disulphide may form within CLIP-associating protein 1 between cysteines 453 and 464.

Details

Redox score ?
62
PDB code
6mq7
Structure name
crystal structure of clasp1 tog2 domain at 1
Structure deposition date
2018-10-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
100
Peptide accession
Q7Z460
Residue number A
453
Residue number B
464
Peptide name
CLIP-associating protein 1

Ligandability

Cysteine 453 of CLIP-associating protein 1

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 464 of CLIP-associating protein 1

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 CLIP-associating protein 1 between cysteines 453 and 509. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6mq7
Structure name
crystal structure of clasp1 tog2 domain at 1
Structure deposition date
2018-10-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
14
% buried
100
Peptide accession
Q7Z460
Residue number A
453
Residue number B
509
Peptide name
CLIP-associating protein 1

Ligandability

Cysteine 453 of CLIP-associating protein 1

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 509 of CLIP-associating protein 1

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 CLIP-associating protein 1 between cysteines 464 and 509. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4k92
Structure name
a cryptic tog domain with a distinct architecture underlies clasp- dependent bipolar spindle formation
Structure deposition date
2013-04-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
14
% buried
nan
Peptide accession
Q7Z460
Residue number A
464
Residue number B
509
Peptide name
CLIP-associating protein 1

Ligandability

Cysteine 464 of CLIP-associating protein 1

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 509 of CLIP-associating protein 1

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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