ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

C-C motif chemokine 14

Intermolecular
Cysteine 35 and cysteine 35
Cysteine 35 and cysteine 59
Cysteine 59 and cysteine 59
Intramolecular
Cysteine 36 and cysteine 75
Cysteine 36 and cysteine 59
Cysteine 35 and cysteine 36
Cysteine 59 and cysteine 75
Cysteine 35 and cysteine 75
A redox-regulated disulphide may form between two units of C-C motif chemokine 14 at cysteines 35 and 35 (16 and 16 respectively in this structure).

Details

Redox score ?
69
PDB code
2q8t
Structure name
crystal structure of the cc chemokine ccl14
Structure deposition date
2007-06-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-C motif chemokine 14
Peptide B name
C-C motif chemokine 14
Peptide A accession
Q16627
Peptide B accession
Q16627
Peptide A residue number
35
Peptide B residue number
35

Ligandability

A redox-regulated disulphide may form between two units of C-C motif chemokine 14 at cysteines 35 and 59 (16 and 40 respectively in this structure).

Details

Redox score ?
62
PDB code
2q8t
Structure name
crystal structure of the cc chemokine ccl14
Structure deposition date
2007-06-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-C motif chemokine 14
Peptide B name
C-C motif chemokine 14
Peptide A accession
Q16627
Peptide B accession
Q16627
Peptide A residue number
35
Peptide B residue number
59

Ligandability

Cysteine 35 of C-C motif chemokine 14

Cysteine 59 of C-C motif chemokine 14

A redox-regulated disulphide may form between two units of C-C motif chemokine 14 at cysteines 59 and 59 (40 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
2q8t
Structure name
crystal structure of the cc chemokine ccl14
Structure deposition date
2007-06-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-C motif chemokine 14
Peptide B name
C-C motif chemokine 14
Peptide A accession
Q16627
Peptide B accession
Q16627
Peptide A residue number
59
Peptide B residue number
59

Ligandability

A redox-regulated disulphide may form within C-C motif chemokine 14 between cysteines 36 and 75 (9 and 48 respectively in this structure).

Details

Redox score ?
81
PDB code
2q8r
Structure name
structural and functional characterization of cc chemokine ccl14
Structure deposition date
2007-06-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16627
Residue number A
36
Residue number B
75
Peptide name
C-C motif chemokine 14

Ligandability

Cysteine 36 of C-C motif chemokine 14

Cysteine 75 of C-C motif chemokine 14

A redox-regulated disulphide may form within C-C motif chemokine 14 between cysteines 36 and 59 (9 and 32 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
2q8r
Structure name
structural and functional characterization of cc chemokine ccl14
Structure deposition date
2007-06-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16627
Residue number A
36
Residue number B
59
Peptide name
C-C motif chemokine 14

Ligandability

Cysteine 36 of C-C motif chemokine 14

Cysteine 59 of C-C motif chemokine 14

A redox-regulated disulphide may form within C-C motif chemokine 14 between cysteines 35 and 36 (16 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2q8t
Structure name
crystal structure of the cc chemokine ccl14
Structure deposition date
2007-06-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16627
Residue number A
35
Residue number B
36
Peptide name
C-C motif chemokine 14

Ligandability

Cysteine 35 of C-C motif chemokine 14

Cysteine 36 of C-C motif chemokine 14

A redox-regulated disulphide may form within C-C motif chemokine 14 between cysteines 59 and 75 (32 and 48 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2q8r
Structure name
structural and functional characterization of cc chemokine ccl14
Structure deposition date
2007-06-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16627
Residue number A
59
Residue number B
75
Peptide name
C-C motif chemokine 14

Ligandability

Cysteine 59 of C-C motif chemokine 14

Cysteine 75 of C-C motif chemokine 14

A redox-regulated disulphide may form within C-C motif chemokine 14 between cysteines 35 and 75 (16 and 56 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2q8t
Structure name
crystal structure of the cc chemokine ccl14
Structure deposition date
2007-06-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16627
Residue number A
35
Residue number B
75
Peptide name
C-C motif chemokine 14

Ligandability

Cysteine 35 of C-C motif chemokine 14

Cysteine 75 of C-C motif chemokine 14

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