C-C motif chemokine 16
Intermolecular
Cysteine 37 and cysteine 37
Cysteine 37 and cysteine 60
Cysteine 60 and cysteine 60
Intramolecular
Cysteine 38 and cysteine 76
Cysteine 38 and cysteine 60
Cysteine 37 and cysteine 38
Cysteine 60 and cysteine 76
Cysteine 37 and cysteine 76
5ltl A 14 B 14
A redox-regulated disulphide may form between two units of C-C motif chemokine 16 at cysteines 37 and 37 (14 and 14 respectively in this structure).
Details
Redox score ?
61
PDB code
5ltl
Structure name
structure of human chemokine ccl16
Structure deposition date
2016-09-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-C motif chemokine 16
Peptide B name
C-C motif chemokine 16
Peptide A accession
O15467
Peptide B accession
O15467
Peptide A residue number
37
Peptide B residue number
37
Ligandability
5ltl A 14 B 37
A redox-regulated disulphide may form between two units of C-C motif chemokine 16 at cysteines 37 and 60 (14 and 37 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
5ltl
Structure name
structure of human chemokine ccl16
Structure deposition date
2016-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-C motif chemokine 16
Peptide B name
C-C motif chemokine 16
Peptide A accession
O15467
Peptide B accession
O15467
Peptide A residue number
37
Peptide B residue number
60
Ligandability
Cysteine 37 of C-C motif chemokine 16
Cysteine 60 of C-C motif chemokine 16
5ltl A 37 B 37
A redox-regulated disulphide may form between two units of C-C motif chemokine 16 at cysteines 60 and 60 (37 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5ltl
Structure name
structure of human chemokine ccl16
Structure deposition date
2016-09-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
C-C motif chemokine 16
Peptide B name
C-C motif chemokine 16
Peptide A accession
O15467
Peptide B accession
O15467
Peptide A residue number
60
Peptide B residue number
60
Ligandability
5ltl A 15 A 53
A redox-regulated disulphide may form within C-C motif chemokine 16 between cysteines 38 and 76 (15 and 53 respectively in this structure).
Details
Redox score ?
82
PDB code
5ltl
Structure name
structure of human chemokine ccl16
Structure deposition date
2016-09-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O15467
Residue number A
38
Residue number B
76
Peptide name
C-C motif chemokine 16
Ligandability
Cysteine 38 of C-C motif chemokine 16
Cysteine 76 of C-C motif chemokine 16
5ltl A 15 A 37
A redox-regulated disulphide may form within C-C motif chemokine 16 between cysteines 38 and 60 (15 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
5ltl
Structure name
structure of human chemokine ccl16
Structure deposition date
2016-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
O15467
Residue number A
38
Residue number B
60
Peptide name
C-C motif chemokine 16
Ligandability
Cysteine 38 of C-C motif chemokine 16
Cysteine 60 of C-C motif chemokine 16
5ltl B 14 B 15
A redox-regulated disulphide may form within C-C motif chemokine 16 between cysteines 37 and 38 (14 and 15 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5ltl
Structure name
structure of human chemokine ccl16
Structure deposition date
2016-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O15467
Residue number A
37
Residue number B
38
Peptide name
C-C motif chemokine 16
Ligandability
Cysteine 37 of C-C motif chemokine 16
Cysteine 38 of C-C motif chemokine 16
5ltl A 37 A 53
A redox-regulated disulphide may form within C-C motif chemokine 16 between cysteines 60 and 76 (37 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5ltl
Structure name
structure of human chemokine ccl16
Structure deposition date
2016-09-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
O15467
Residue number A
60
Residue number B
76
Peptide name
C-C motif chemokine 16
Ligandability
Cysteine 60 of C-C motif chemokine 16
Cysteine 76 of C-C motif chemokine 16
5ltl B 14 B 53
A redox-regulated disulphide may form within C-C motif chemokine 16 between cysteines 37 and 76 (14 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5ltl
Structure name
structure of human chemokine ccl16
Structure deposition date
2016-09-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O15467
Residue number A
37
Residue number B
76
Peptide name
C-C motif chemokine 16
Ligandability
Cysteine 37 of C-C motif chemokine 16
Cysteine 76 of C-C motif chemokine 16
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