Protein AF-9
Intermolecular
Cysteine 119 and cysteine 119
Cysteine 5 and cysteine 5
Intramolecular
Cysteine 499 and cysteine 548
5hjd C 119 E 119
A redox-regulated disulphide may form between two units of Protein AF-9 at cysteines 119 and 119.
Details
Redox score ?
84
PDB code
5hjd
Structure name
af9 yeats in complex with histone h3 crotonylation at k18
Structure deposition date
2016-01-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Protein AF-9
Peptide B name
Protein AF-9
Peptide A accession
P42568
Peptide B accession
P42568
Peptide A residue number
119
Peptide B residue number
119
Ligandability
4tmp A 5 C 5
A redox-regulated disulphide may form between two units of Protein AF-9 at cysteines 5 and 5.
Details
Redox score ?
80
PDB code
4tmp
Structure name
crystal structure of af9 yeats bound to h3k9ac peptide
Structure deposition date
2014-06-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
7
% buried
58
Peptide A name
Protein AF-9
Peptide B name
Protein AF-9
Peptide A accession
P42568
Peptide B accession
P42568
Peptide A residue number
5
Peptide B residue number
5
Ligandability
2lm0 A 1499 A 1548
A redox-regulated disulphide may form within Protein AF-9 between cysteines 499 and 548 (1499 and 1548 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2lm0
Structure name
solution structure of the af4-af9 complex
Structure deposition date
2011-11-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
37
Minimum pKa ?
9
% buried
14
Peptide accession
P42568
Residue number A
499
Residue number B
548
Peptide name
Protein AF-9
Ligandability
Cysteine 499 of Protein AF-9
Cysteine 548 of Protein AF-9
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