C-X-C motif chemokine
Intramolecular
Cysteine 43 and cysteine 69
Cysteine 45 and cysteine 85
Cysteine 45 and cysteine 69
Cysteine 43 and cysteine 45
Cysteine 69 and cysteine 85
Cysteine 43 and cysteine 85
6wzj E 9 E 35
A redox-regulated disulphide may form within C-X-C motif chemokine between cysteines 43 and 69 (9 and 35 respectively in this structure).
Details
Redox score ?
83
PDB code
6wzj
Structure name
ly3041658 fab bound to cxcl2
Structure deposition date
2020-05-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q0EAC2
Residue number A
43
Residue number B
69
Peptide name
C-X-C motif chemokine
Ligandability
Cysteine 43 of C-X-C motif chemokine
Cysteine 69 of C-X-C motif chemokine
6wzj E 11 E 51
A redox-regulated disulphide may form within C-X-C motif chemokine between cysteines 45 and 85 (11 and 51 respectively in this structure).
Details
Redox score ?
81
PDB code
6wzj
Structure name
ly3041658 fab bound to cxcl2
Structure deposition date
2020-05-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q0EAC2
Residue number A
45
Residue number B
85
Peptide name
C-X-C motif chemokine
Ligandability
Cysteine 45 of C-X-C motif chemokine
Cysteine 85 of C-X-C motif chemokine
6wzj F 11 F 35
A redox-regulated disulphide may form within C-X-C motif chemokine between cysteines 45 and 69 (11 and 35 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
6wzj
Structure name
ly3041658 fab bound to cxcl2
Structure deposition date
2020-05-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q0EAC2
Residue number A
45
Residue number B
69
Peptide name
C-X-C motif chemokine
Ligandability
Cysteine 45 of C-X-C motif chemokine
Cysteine 69 of C-X-C motif chemokine
6wzj F 9 F 11
A redox-regulated disulphide may form within C-X-C motif chemokine between cysteines 43 and 45 (9 and 11 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
6wzj
Structure name
ly3041658 fab bound to cxcl2
Structure deposition date
2020-05-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q0EAC2
Residue number A
43
Residue number B
45
Peptide name
C-X-C motif chemokine
Ligandability
Cysteine 43 of C-X-C motif chemokine
Cysteine 45 of C-X-C motif chemokine
6wzj E 35 E 51
A redox-regulated disulphide may form within C-X-C motif chemokine between cysteines 69 and 85 (35 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 ?
40
PDB code
6wzj
Structure name
ly3041658 fab bound to cxcl2
Structure deposition date
2020-05-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q0EAC2
Residue number A
69
Residue number B
85
Peptide name
C-X-C motif chemokine
Ligandability
Cysteine 69 of C-X-C motif chemokine
Cysteine 85 of C-X-C motif chemokine
6wzj E 9 E 51
A redox-regulated disulphide may form within C-X-C motif chemokine between cysteines 43 and 85 (9 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 ?
36
PDB code
6wzj
Structure name
ly3041658 fab bound to cxcl2
Structure deposition date
2020-05-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q0EAC2
Residue number A
43
Residue number B
85
Peptide name
C-X-C motif chemokine
Ligandability
Cysteine 43 of C-X-C motif chemokine
Cysteine 85 of C-X-C motif chemokine
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