NK-tumor recognition protein
Intramolecular
Cysteine 58 and cysteine 173
Cysteine 9 and cysteine 43
Cysteine 43 and cysteine 173
Cysteine 32 and cysteine 36
Cysteine 9 and cysteine 173
Cysteine 43 and cysteine 58
Cysteine 9 and cysteine 36
Cysteine 41 and cysteine 43
2he9 B 58 B 173
A redox-regulated disulphide may form within NK-tumor recognition protein between cysteines 58 and 173.
Details
Redox score ?
77
PDB code
2he9
Structure name
structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein
Structure deposition date
2006-06-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
6
% buried
52
Peptide accession
P30414
Residue number A
58
Residue number B
173
Peptide name
NK-tumor recognition protein
Ligandability
Cysteine 58 of NK-tumor recognition protein
Cysteine 173 of NK-tumor recognition protein
2he9 B 9 B 43
A redox-regulated disulphide may form within NK-tumor recognition protein between cysteines 9 and 43.
Details
Redox score ?
69
PDB code
2he9
Structure name
structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein
Structure deposition date
2006-06-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
95
Peptide accession
P30414
Residue number A
9
Residue number B
43
Peptide name
NK-tumor recognition protein
Ligandability
Cysteine 9 of NK-tumor recognition protein
Cysteine 43 of NK-tumor recognition protein
2he9 B 43 B 173
A redox-regulated disulphide may form within NK-tumor recognition protein between cysteines 43 and 173. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2he9
Structure name
structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein
Structure deposition date
2006-06-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
16
% buried
80
Peptide accession
P30414
Residue number A
43
Residue number B
173
Peptide name
NK-tumor recognition protein
Ligandability
Cysteine 43 of NK-tumor recognition protein
Cysteine 173 of NK-tumor recognition protein
2he9 A 32 A 36
A redox-regulated disulphide may form within NK-tumor recognition protein between cysteines 32 and 36. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2he9
Structure name
structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein
Structure deposition date
2006-06-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
98
Peptide accession
P30414
Residue number A
32
Residue number B
36
Peptide name
NK-tumor recognition protein
Ligandability
Cysteine 32 of NK-tumor recognition protein
Cysteine 36 of NK-tumor recognition protein
2he9 B 9 B 173
A redox-regulated disulphide may form within NK-tumor recognition protein between cysteines 9 and 173. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2he9
Structure name
structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein
Structure deposition date
2006-06-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
76
Peptide accession
P30414
Residue number A
9
Residue number B
173
Peptide name
NK-tumor recognition protein
Ligandability
Cysteine 9 of NK-tumor recognition protein
Cysteine 173 of NK-tumor recognition protein
2he9 A 43 A 58
A redox-regulated disulphide may form within NK-tumor recognition protein between cysteines 43 and 58. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2he9
Structure name
structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein
Structure deposition date
2006-06-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
71
Peptide accession
P30414
Residue number A
43
Residue number B
58
Peptide name
NK-tumor recognition protein
Ligandability
Cysteine 43 of NK-tumor recognition protein
Cysteine 58 of NK-tumor recognition protein
2he9 A 9 A 36
A redox-regulated disulphide may form within NK-tumor recognition protein between cysteines 9 and 36. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2he9
Structure name
structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein
Structure deposition date
2006-06-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
94
Peptide accession
P30414
Residue number A
9
Residue number B
36
Peptide name
NK-tumor recognition protein
Ligandability
Cysteine 9 of NK-tumor recognition protein
Cysteine 36 of NK-tumor recognition protein
2he9 B 41 B 43
A redox-regulated disulphide may form within NK-tumor recognition protein between cysteines 41 and 43. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
2he9
Structure name
structure of the peptidylprolyl isomerase domain of the human nk- tumour recognition protein
Structure deposition date
2006-06-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
65
Peptide accession
P30414
Residue number A
41
Residue number B
43
Peptide name
NK-tumor recognition protein
Ligandability
Cysteine 41 of NK-tumor recognition protein
Cysteine 43 of NK-tumor recognition protein
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