Retinol-binding protein 4
Intramolecular
Cysteine 22 and cysteine 178
Cysteine 70 and cysteine 174
Cysteine 120 and cysteine 129
Cysteine 22 and cysteine 138
Cysteine 129 and cysteine 160
Cysteine 22 and cysteine 147
Cysteine 120 and cysteine 160
1aqb A 4 A 160
A redox-regulated disulphide may form within Retinol-binding protein 4 between cysteines 22 and 178 (4 and 160 respectively in this structure).
Details
Redox score ?
84
PDB code
1aqb
Structure name
retinol-binding protein (rbp) from pig plasma
Structure deposition date
1997-07-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27485
Residue number A
22
Residue number B
178
Peptide name
Retinol-binding protein 4
Ligandability
Cysteine 22 of Retinol-binding protein 4
Cysteine 178 of Retinol-binding protein 4
1fem A 70 A 174
A redox-regulated disulphide may form within Retinol-binding protein 4 between cysteines 70 and 174.
Details
Redox score ?
81
PDB code
1fem
Structure name
crystallographic studies on complexes between retinoids and plasma retinol-binding protein
Structure deposition date
1994-08-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
18
Peptide accession
P18902
Residue number A
70
Residue number B
174
Peptide name
Retinol-binding protein 4
Ligandability
Cysteine 70 of Retinol-binding protein 4
Cysteine 174 of Retinol-binding protein 4
1fen A 120 A 129
A redox-regulated disulphide may form within Retinol-binding protein 4 between cysteines 120 and 129.
Details
Redox score ?
80
PDB code
1fen
Structure name
crystallographic studies on complexes between retinoids and plasma retinol-binding protein
Structure deposition date
1994-08-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
39
Peptide accession
P18902
Residue number A
120
Residue number B
129
Peptide name
Retinol-binding protein 4
Ligandability
Cysteine 120 of Retinol-binding protein 4
Cysteine 129 of Retinol-binding protein 4
1qab F 4 F 120
A redox-regulated disulphide may form within Retinol-binding protein 4 between cysteines 22 and 138 (4 and 120 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
1qab
Structure name
the structure of human retinol binding protein with its carrier protein transthyretin reveals interaction with the carboxy terminus of rbp
Structure deposition date
1999-02-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02753
Residue number A
22
Residue number B
138
Peptide name
Retinol-binding protein 4
Ligandability
Cysteine 22 of Retinol-binding protein 4
Cysteine 138 of Retinol-binding protein 4
1fem A 129 A 160
A redox-regulated disulphide may form within Retinol-binding protein 4 between cysteines 129 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
1fem
Structure name
crystallographic studies on complexes between retinoids and plasma retinol-binding protein
Structure deposition date
1994-08-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
37
Peptide accession
P18902
Residue number A
129
Residue number B
160
Peptide name
Retinol-binding protein 4
Ligandability
Cysteine 129 of Retinol-binding protein 4
Cysteine 160 of Retinol-binding protein 4
2wqa E 4 E 129
A redox-regulated disulphide may form within Retinol-binding protein 4 between cysteines 22 and 147 (4 and 129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2wqa
Structure name
complex of ttr and rbp4 and oleic acid
Structure deposition date
2009-08-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
nan
Peptide accession
P02753
Residue number A
22
Residue number B
147
Peptide name
Retinol-binding protein 4
Ligandability
Cysteine 22 of Retinol-binding protein 4
Cysteine 147 of Retinol-binding protein 4
1fem A 120 A 160
A redox-regulated disulphide may form within Retinol-binding protein 4 between cysteines 120 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
1fem
Structure name
crystallographic studies on complexes between retinoids and plasma retinol-binding protein
Structure deposition date
1994-08-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
32
Peptide accession
P18902
Residue number A
120
Residue number B
160
Peptide name
Retinol-binding protein 4
Ligandability
Cysteine 120 of Retinol-binding protein 4
Cysteine 160 of Retinol-binding protein 4
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