ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Evasin-1

Intermolecular
Cysteine 53 and cysteine 73 of C-C motif chemokine 3
Cysteine 32 and cysteine 73 of C-C motif chemokine 3
Cysteine 32 and cysteine 34 of C-C motif chemokine 3
A redox-regulated disulphide may form between cysteine 53 of Evasin-1 and cysteine 73 of C-C motif chemokine 3 (33 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3fpu
Structure name
the crystallographic structure of the complex between evasin-1 and ccl3
Structure deposition date
2009-01-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide A name
Evasin-1
Peptide B name
C-C motif chemokine 3
Peptide A accession
P0C8E7
Peptide B accession
P10147
Peptide A residue number
53
Peptide B residue number
73

Ligandability

Cysteine 53 of Evasin-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 73 of C-C motif chemokine 3

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 between cysteine 32 of Evasin-1 and cysteine 73 of C-C motif chemokine 3 (12 and 51 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3fpu
Structure name
the crystallographic structure of the complex between evasin-1 and ccl3
Structure deposition date
2009-01-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Evasin-1
Peptide B name
C-C motif chemokine 3
Peptide A accession
P0C8E7
Peptide B accession
P10147
Peptide A residue number
32
Peptide B residue number
73

Ligandability

Cysteine 32 of Evasin-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 73 of C-C motif chemokine 3

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 between cysteine 32 of Evasin-1 and cysteine 34 of C-C motif chemokine 3 (12 and 12 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3fpu
Structure name
the crystallographic structure of the complex between evasin-1 and ccl3
Structure deposition date
2009-01-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Evasin-1
Peptide B name
C-C motif chemokine 3
Peptide A accession
P0C8E7
Peptide B accession
P10147
Peptide A residue number
32
Peptide B residue number
34

Ligandability

Cysteine 32 of Evasin-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 34 of C-C motif chemokine 3

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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