Filamin-A
Intermolecular
Cysteine 59 and cysteine 59
Intramolecular
Cysteine 59 and cysteine 2199 L
Cysteine 2160 and cysteine 2199 L
Cysteine 1912 and cysteine 1920 L
Cysteine 623 and cysteine 631
Cysteine 478 and cysteine 483 L
Cysteine 1165 and cysteine 1185 L
Cysteine 2476 and cysteine 2479 L
Cysteine 205 and cysteine 210
3hor A 59 B 59
A redox-regulated disulphide may form between two units of Filamin-A at cysteines 59 and 59.
Details
Redox score ?
82
PDB code
3hor
Structure name
structure of the actin-binding domain of human filamin a (reduced)
Structure deposition date
2009-06-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
19
Peptide A name
Filamin-A
Peptide B name
Filamin-A
Peptide A accession
P21333
Peptide B accession
P21333
Peptide A residue number
59
Peptide B residue number
59
Ligandability
4p3w F 2160 F 2199
A redox-regulated disulphide may form within Filamin-A between cysteines 59 and 2199 (2160 and 2199 respectively in this structure).
Details
Redox score ?
89
PDB code
4p3w
Structure name
crystal structure of the human filamin a ig-like domains 20-21 in complex with migfilin peptide
Structure deposition date
2014-03-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21333
Residue number A
59
Residue number B
2199
Peptide name
Filamin-A
Ligandability
Cysteine 59 of Filamin-A
Cysteine 2199 of Filamin-A
2j3s A 2160 A 2199
A redox-regulated disulphide may form within Filamin-A between cysteines 2160 and 2199.
Details
Redox score ?
85
PDB code
2j3s
Structure name
crystal structure of the human filamin a ig domains 19 to 21
Structure deposition date
2006-08-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
33
Minimum pKa ?
9
% buried
0
Peptide accession
P21333
Residue number A
2160
Residue number B
2199
Peptide name
Filamin-A
Ligandability
Cysteine 2160 of Filamin-A
Cysteine 2199 of Filamin-A
2bp3 B 1912 B 1920
A redox-regulated disulphide may form within Filamin-A between cysteines 1912 and 1920.
Details
Redox score ?
77
PDB code
2bp3
Structure name
crystal structure of filamin a domain 17 and gpib alpha cytoplasmic domain complex
Structure deposition date
2005-04-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
46
Peptide accession
P21333
Residue number A
1912
Residue number B
1920
Peptide name
Filamin-A
Ligandability
Cysteine 1912 of Filamin-A
Cysteine 1920 of Filamin-A
4m9p A 623 A 631
A redox-regulated disulphide may form within Filamin-A between cysteines 623 and 631.
Details
Redox score ?
67
PDB code
4m9p
Structure name
crystal structure of the human filamin a ig-like domains 3-5
Structure deposition date
2013-08-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
32
Peptide accession
P21333
Residue number A
623
Residue number B
631
Peptide name
Filamin-A
Ligandability
Cysteine 623 of Filamin-A
Cysteine 631 of Filamin-A
4m9p A 478 A 483
A redox-regulated disulphide may form within Filamin-A between cysteines 478 and 483. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
4m9p
Structure name
crystal structure of the human filamin a ig-like domains 3-5
Structure deposition date
2013-08-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
nan
Peptide accession
P21333
Residue number A
478
Residue number B
483
Peptide name
Filamin-A
Ligandability
Cysteine 478 of Filamin-A
Cysteine 483 of Filamin-A
3rgh A 165 A 185
A redox-regulated disulphide may form within Filamin-A between cysteines 1165 and 1185 (165 and 185 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
3rgh
Structure name
structure of filamin a immunoglobulin-like repeat 10 from homo sapiens
Structure deposition date
2011-04-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
60
Peptide accession
P21333
Residue number A
1165
Residue number B
1185
Peptide name
Filamin-A
Ligandability
Cysteine 1165 of Filamin-A
Cysteine 1185 of Filamin-A
2k3t A 2476 A 2479
A redox-regulated disulphide may form within Filamin-A between cysteines 2476 and 2479. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2k3t
Structure name
solution structure of ig-like domain 23 from human filamin a
Structure deposition date
2008-05-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
38
Minimum pKa ?
9
% buried
10
Peptide accession
P21333
Residue number A
2476
Residue number B
2479
Peptide name
Filamin-A
Ligandability
Cysteine 2476 of Filamin-A
Cysteine 2479 of Filamin-A
3hoc A 205 A 210
A redox-regulated disulphide may form within Filamin-A between cysteines 205 and 210. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3hoc
Structure name
structure of the actin-binding domain of human filamin a mutant e254k
Structure deposition date
2009-06-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
50
Peptide accession
P21333
Residue number A
205
Residue number B
210
Peptide name
Filamin-A
Ligandability
Cysteine 205 of Filamin-A
Cysteine 210 of Filamin-A
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