APOBEC3H
Intermolecular
Cysteine 85 and cysteine 85
Cysteine 116 and cysteine 85
Cysteine 116 and cysteine 88
Intramolecular
Cysteine 53 and cysteine 58
Cysteine 31 and cysteine 144
Cysteine 85 and cysteine 88
Cysteine 31 and cysteine 78
Cysteine 58 and cysteine 88
Cysteine 53 and cysteine 88
Cysteine 78 and cysteine 144
6b0b A 85 E 85
A redox-regulated disulphide may form between two units of APOBEC3H at cysteines 85 and 85. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
6b0b
Structure name
crystal structure of human apobec3h
Structure deposition date
2017-09-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
APOBEC3H
Peptide B name
APOBEC3H
Peptide A accession
B7TQM6
Peptide B accession
B7TQM6
Peptide A residue number
85
Peptide B residue number
85
Ligandability
6bbo A 116 E 85
A redox-regulated disulphide may form between two units of APOBEC3H at cysteines 116 and 85. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
6bbo
Structure name
crystal structure of human apobec3h/rna complex
Structure deposition date
2017-10-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
13
% buried
nan
Peptide A name
APOBEC3H
Peptide B name
APOBEC3H
Peptide A accession
B7TQM6
Peptide B accession
B7TQM6
Peptide A residue number
116
Peptide B residue number
85
Ligandability
Cysteine 116 of APOBEC3H
Cysteine 85 of APOBEC3H
6b0b A 116 E 88
A redox-regulated disulphide may form between two units of APOBEC3H at cysteines 116 and 88. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
6b0b
Structure name
crystal structure of human apobec3h
Structure deposition date
2017-09-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
13
% buried
90
Peptide A name
APOBEC3H
Peptide B name
APOBEC3H
Peptide A accession
B7TQM6
Peptide B accession
B7TQM6
Peptide A residue number
116
Peptide B residue number
88
Ligandability
Cysteine 116 of APOBEC3H
Cysteine 88 of APOBEC3H
6bbo A 53 A 58
A redox-regulated disulphide may form within APOBEC3H between cysteines 53 and 58.
Details
Redox score ?
76
PDB code
6bbo
Structure name
crystal structure of human apobec3h/rna complex
Structure deposition date
2017-10-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
58
Peptide accession
B7TQM6
Residue number A
53
Residue number B
58
Peptide name
APOBEC3H
Ligandability
Cysteine 53 of APOBEC3H
Cysteine 58 of APOBEC3H
6bbo E 31 E 144
A redox-regulated disulphide may form within APOBEC3H between cysteines 31 and 144.
Details
Redox score ?
69
PDB code
6bbo
Structure name
crystal structure of human apobec3h/rna complex
Structure deposition date
2017-10-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
9
% buried
100
Peptide accession
B7TQM6
Residue number A
31
Residue number B
144
Peptide name
APOBEC3H
Ligandability
Cysteine 31 of APOBEC3H
Cysteine 144 of APOBEC3H
6b0b A 85 A 88
A redox-regulated disulphide may form within APOBEC3H between cysteines 85 and 88. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6b0b
Structure name
crystal structure of human apobec3h
Structure deposition date
2017-09-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
16
% buried
nan
Peptide accession
B7TQM6
Residue number A
85
Residue number B
88
Peptide name
APOBEC3H
Ligandability
Cysteine 85 of APOBEC3H
Cysteine 88 of APOBEC3H
6b0b A 31 A 78
A redox-regulated disulphide may form within APOBEC3H between cysteines 31 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6b0b
Structure name
crystal structure of human apobec3h
Structure deposition date
2017-09-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
100
Peptide accession
B7TQM6
Residue number A
31
Residue number B
78
Peptide name
APOBEC3H
Ligandability
Cysteine 31 of APOBEC3H
Cysteine 78 of APOBEC3H
6b0b A 58 A 88
A redox-regulated disulphide may form within APOBEC3H between cysteines 58 and 88. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6b0b
Structure name
crystal structure of human apobec3h
Structure deposition date
2017-09-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
74
Peptide accession
B7TQM6
Residue number A
58
Residue number B
88
Peptide name
APOBEC3H
Ligandability
Cysteine 58 of APOBEC3H
Cysteine 88 of APOBEC3H
6bbo A 53 A 88
A redox-regulated disulphide may form within APOBEC3H between cysteines 53 and 88. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6bbo
Structure name
crystal structure of human apobec3h/rna complex
Structure deposition date
2017-10-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
14
% buried
84
Peptide accession
B7TQM6
Residue number A
53
Residue number B
88
Peptide name
APOBEC3H
Ligandability
Cysteine 53 of APOBEC3H
Cysteine 88 of APOBEC3H
6b0b A 78 A 144
A redox-regulated disulphide may form within APOBEC3H between cysteines 78 and 144. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
6b0b
Structure name
crystal structure of human apobec3h
Structure deposition date
2017-09-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
B7TQM6
Residue number A
78
Residue number B
144
Peptide name
APOBEC3H
Ligandability
Cysteine 78 of APOBEC3H
Cysteine 144 of APOBEC3H
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