Superoxide dismutase [Cu-Zn]
Intermolecular
Cysteine 147 and cysteine 231 of Superoxide dismutase 1 copper chaperone L
Cysteine 58 and cysteine 231 of Superoxide dismutase 1 copper chaperone
Cysteine 7 and cysteine 7
Cysteine 112 and cysteine 112
Cysteine 147 and cysteine 147 L
Intramolecular
Cysteine 58 and cysteine 147 L
Cysteine 7 and cysteine 58
Cysteine 7 and cysteine 147 L
Cysteine 112 and cysteine 201
5u9m A 146 B 231
A redox-regulated disulphide may form between cysteine 147 of Superoxide dismutase [Cu-Zn] and cysteine 231 of Superoxide dismutase 1 copper chaperone (146 and 231 respectively in this structure).
Details
Redox score ?
77
PDB code
5u9m
Structure name
copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper-ion entry site
Structure deposition date
2016-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
82
Peptide A name
Superoxide dismutase [Cu-Zn]
Peptide B name
Superoxide dismutase 1 copper chaperone
Peptide A accession
P00441
Peptide B accession
P40202
Peptide A residue number
147
Peptide B residue number
231
Ligandability
Cysteine 147 of Superoxide dismutase [Cu-Zn]
Cysteine 231 of Superoxide dismutase 1 copper chaperone
5u9m A 57 B 231
A redox-regulated disulphide may form between cysteine 58 of Superoxide dismutase [Cu-Zn] and cysteine 231 of Superoxide dismutase 1 copper chaperone (57 and 231 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
5u9m
Structure name
copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper-ion entry site
Structure deposition date
2016-12-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
50
Peptide A name
Superoxide dismutase [Cu-Zn]
Peptide B name
Superoxide dismutase 1 copper chaperone
Peptide A accession
P00441
Peptide B accession
P40202
Peptide A residue number
58
Peptide B residue number
231
Ligandability
Cysteine 58 of Superoxide dismutase [Cu-Zn]
Cysteine 231 of Superoxide dismutase 1 copper chaperone
7vzf A 6 C 6
A redox-regulated disulphide may form between two units of Superoxide dismutase [Cu-Zn] at cysteines 7 and 7 (6 and 6 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7vzf
Structure name
cryo-em structure of amyloid fibril formed by full-length human sod1
Structure deposition date
2021-11-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
22
Peptide A name
Superoxide dismutase [Cu-Zn]
Peptide B name
Superoxide dismutase [Cu-Zn]
Peptide A accession
P00441
Peptide B accession
P00441
Peptide A residue number
7
Peptide B residue number
7
Ligandability
6spi B 111 K 111
A redox-regulated disulphide may form between two units of Superoxide dismutase [Cu-Zn] at cysteines 112 and 112 (111 and 111 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
6spi
Structure name
a4v mutant of human sod1 with ebselen derivative 4
Structure deposition date
2019-09-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
76
Peptide A name
Superoxide dismutase [Cu-Zn]
Peptide B name
Superoxide dismutase [Cu-Zn]
Peptide A accession
P00441
Peptide B accession
P00441
Peptide A residue number
112
Peptide B residue number
112
Ligandability
2af2 A 146 B 146
A redox-regulated disulphide may form between two units of Superoxide dismutase [Cu-Zn] at cysteines 147 and 147 (146 and 146 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
2af2
Structure name
solution structure of disulfide reduced and copper depleted human superoxide dismutase
Structure deposition date
2005-07-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
97
Minimum pKa ?
11
% buried
89
Peptide A name
Superoxide dismutase [Cu-Zn]
Peptide B name
Superoxide dismutase [Cu-Zn]
Peptide A accession
P00441
Peptide B accession
P00441
Peptide A residue number
147
Peptide B residue number
147
Ligandability
3gtv I 57 I 146
A redox-regulated disulphide may form within Superoxide dismutase [Cu-Zn] between cysteines 58 and 147 (57 and 146 respectively in this structure).
Details
Redox score ?
85
PDB code
3gtv
Structure name
human-mouse sod1 chimera
Structure deposition date
2009-03-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
80
Minimum pKa ?
7
% buried
70
Peptide accession
P08228
Residue number A
58
Residue number B
147
Peptide name
Superoxide dismutase [Cu-Zn]
Ligandability
Cysteine 58 of Superoxide dismutase [Cu-Zn]
Cysteine 147 of Superoxide dismutase [Cu-Zn]
3cqq B 6 B 57
A redox-regulated disulphide may form within Superoxide dismutase [Cu-Zn] between cysteines 7 and 58 (6 and 57 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
3cqq
Structure name
human sod1 g85r variant, structure ii
Structure deposition date
2008-04-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
7
% buried
77
Peptide accession
P00441
Residue number A
7
Residue number B
58
Peptide name
Superoxide dismutase [Cu-Zn]
Ligandability
Cysteine 7 of Superoxide dismutase [Cu-Zn]
Cysteine 58 of Superoxide dismutase [Cu-Zn]
3gtv I 6 I 146
A redox-regulated disulphide may form within Superoxide dismutase [Cu-Zn] between cysteines 7 and 147 (6 and 146 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
3gtv
Structure name
human-mouse sod1 chimera
Structure deposition date
2009-03-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
95
Minimum pKa ?
13
% buried
91
Peptide accession
P08228
Residue number A
7
Residue number B
147
Peptide name
Superoxide dismutase [Cu-Zn]
Ligandability
Cysteine 7 of Superoxide dismutase [Cu-Zn]
Cysteine 147 of Superoxide dismutase [Cu-Zn]
4ff9 A 111 A 201
A redox-regulated disulphide may form within Superoxide dismutase [Cu-Zn] between cysteines 112 and 201 (111 and 201 respectively in this structure).
Details
Redox score ?
nan
PDB code
4ff9
Structure name
crystal structure of cysteinylated wt sod1
Structure deposition date
2012-05-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide accession
P00441
Residue number A
112
Residue number B
201
Peptide name
Superoxide dismutase [Cu-Zn]
Ligandability
Cysteine 112 of Superoxide dismutase [Cu-Zn]
Cysteine 201 of Superoxide dismutase [Cu-Zn]
Cysteine 201 in protein B could not be asigned to a Uniprot residue.
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