Protein 4.1
Intramolecular
Cysteine 212 and cysteine 224
Cysteine 224 and cysteine 240
Cysteine 416 and cysteine 480
Cysteine 212 and cysteine 240
1gg3 B 3 B 15
A redox-regulated disulphide may form within Protein 4.1 between cysteines 212 and 224 (3 and 15 respectively in this structure).
Details
Redox score ?
69
PDB code
1gg3
Structure name
crystal structure of the protein 4
Structure deposition date
2000-07-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
55
Peptide accession
P11171
Residue number A
212
Residue number B
224
Peptide name
Protein 4
Ligandability
Cysteine 212 of Protein 4.1
Cysteine 224 of Protein 4.1
1gg3 C 15 C 31
A redox-regulated disulphide may form within Protein 4.1 between cysteines 224 and 240 (15 and 31 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
1gg3
Structure name
crystal structure of the protein 4
Structure deposition date
2000-07-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
64
Peptide accession
P11171
Residue number A
224
Residue number B
240
Peptide name
Protein 4
Ligandability
Cysteine 224 of Protein 4.1
Cysteine 240 of Protein 4.1
3qij B 416 B 480
A redox-regulated disulphide may form within Protein 4.1 between cysteines 416 and 480. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
3qij
Structure name
primitive-monoclinic crystal structure of the ferm domain of protein 4
Structure deposition date
2011-01-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P11171
Residue number A
416
Residue number B
480
Peptide name
Protein 4
Ligandability
Cysteine 416 of Protein 4.1
Cysteine 480 of Protein 4.1
1gg3 A 3 A 31
A redox-regulated disulphide may form within Protein 4.1 between cysteines 212 and 240 (3 and 31 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
1gg3
Structure name
crystal structure of the protein 4
Structure deposition date
2000-07-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
13
% buried
83
Peptide accession
P11171
Residue number A
212
Residue number B
240
Peptide name
Protein 4
Ligandability
Cysteine 212 of Protein 4.1
Cysteine 240 of Protein 4.1
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