Ferritin heavy chain
Intermolecular
Cysteine 131 and cysteine 131
Intramolecular
Cysteine 91 and cysteine 103
Cysteine 103 and cysteine 106
Cysteine 64 and cysteine 140
5jkm G 130 I 130
A redox-regulated disulphide may form between two units of Ferritin heavy chain at cysteines 131 and 131 (130 and 130 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5jkm
Structure name
binary crystal structure of positively and negatively supercharged variants ftn(pos) and ftn(neg) from human heavy chain ferritin (mg acetate condition)
Structure deposition date
2016-04-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
58
Peptide A name
Ferritin heavy chain
Peptide B name
Ferritin heavy chain
Peptide A accession
P02794
Peptide B accession
P02794
Peptide A residue number
131
Peptide B residue number
131
Ligandability
6job K 90 K 102
A redox-regulated disulphide may form within Ferritin heavy chain between cysteines 91 and 103 (90 and 102 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
6job
Structure name
ferritin variant with "gmg" motif
Structure deposition date
2019-03-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
36
Peptide accession
P02794
Residue number A
91
Residue number B
103
Peptide name
Ferritin heavy chain
Ligandability
Cysteine 91 of Ferritin heavy chain
Cysteine 103 of Ferritin heavy chain
7u5l X 103 X 106
A redox-regulated disulphide may form within Ferritin heavy chain between cysteines 103 and 106. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
7u5l
Structure name
cryo-em structure of ferritin
Structure deposition date
2022-03-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
36
Peptide accession
O46414
Residue number A
103
Residue number B
106
Peptide name
Ferritin heavy chain
Ligandability
Cysteine 103 of Ferritin heavy chain
Cysteine 106 of Ferritin heavy chain
3erz J 64 J 140
A redox-regulated disulphide may form within Ferritin heavy chain between cysteines 64 and 140.
Details
Redox score ?
nan
PDB code
3erz
Structure name
directing noble metal ion chemistry within a designed ferritin protein
Structure deposition date
2008-10-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
26
Peptide accession
P02794
Residue number A
64
Residue number B
140
Peptide name
Ferritin heavy chain
Ligandability
Cysteine 64 of Ferritin heavy chain
Cysteine 140 of Ferritin heavy chain
Cysteine 64 in protein A could not be asigned to a Uniprot residue.
Cysteine 140 in protein B could not be asigned to a Uniprot residue.
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