Vitamin D-binding protein
Intramolecular
Cysteine 335 and cysteine 376
Cysteine 189 and cysteine 198
Cysteine 111 and cysteine 122
Cysteine 74 and cysteine 83
Cysteine 29 and cysteine 75
Cysteine 145 and cysteine 190
Cysteine 286 and cysteine 300
Cysteine 96 and cysteine 112
Cysteine 265 and cysteine 273
Cysteine 452 and cysteine 462
More...Cysteine 220 and cysteine 266
Cysteine 407 and cysteine 453
Cysteine 375 and cysteine 384
Cysteine 299 and cysteine 311
Cysteine 111 and cysteine 112
Cysteine 375 and cysteine 376
Cysteine 29 and cysteine 74
Cysteine 74 and cysteine 75
Cysteine 265 and cysteine 266
Cysteine 189 and cysteine 190
Cysteine 299 and cysteine 300
Cysteine 96 and cysteine 111
Cysteine 452 and cysteine 453
Cysteine 145 and cysteine 189
Cysteine 300 and cysteine 311
Cysteine 75 and cysteine 83
Cysteine 286 and cysteine 299
Cysteine 407 and cysteine 452
Cysteine 190 and cysteine 198
Cysteine 376 and cysteine 384
Cysteine 29 and cysteine 83
Cysteine 220 and cysteine 265
Cysteine 335 and cysteine 375
Cysteine 453 and cysteine 462
Cysteine 286 and cysteine 311
Cysteine 407 and cysteine 462
Cysteine 220 and cysteine 273
Cysteine 335 and cysteine 384
Cysteine 96 and cysteine 122
Cysteine 112 and cysteine 122
1j7e B 319 B 360
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 335 and 376 (319 and 360 respectively in this structure).
Details
Redox score ?
86
PDB code
1j7e
Structure name
a structural basis for the unique binding features of the human vitamin d-binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
335
Residue number B
376
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 335 of Vitamin D-binding protein
Cysteine 376 of Vitamin D-binding protein
1j7e B 173 B 182
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 189 and 198 (173 and 182 respectively in this structure).
Details
Redox score ?
85
PDB code
1j7e
Structure name
a structural basis for the unique binding features of the human vitamin d-binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
189
Residue number B
198
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 189 of Vitamin D-binding protein
Cysteine 198 of Vitamin D-binding protein
1kw2 A 111 A 122
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 111 and 122.
Details
Redox score ?
85
PDB code
1kw2
Structure name
crystal structure of uncomplexed vitamin d-binding protein
Structure deposition date
2002-01-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
111
Residue number B
122
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 111 of Vitamin D-binding protein
Cysteine 122 of Vitamin D-binding protein
1kxp D 74 D 83
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 74 and 83.
Details
Redox score ?
84
PDB code
1kxp
Structure name
crystal structure of human vitamin d-binding protein in complex with skeletal actin
Structure deposition date
2002-02-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
74
Residue number B
83
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 74 of Vitamin D-binding protein
Cysteine 83 of Vitamin D-binding protein
1kxp D 29 D 75
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 29 and 75.
Details
Redox score ?
84
PDB code
1kxp
Structure name
crystal structure of human vitamin d-binding protein in complex with skeletal actin
Structure deposition date
2002-02-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
29
Residue number B
75
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 29 of Vitamin D-binding protein
Cysteine 75 of Vitamin D-binding protein
1lot A 129 A 174
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 145 and 190 (129 and 174 respectively in this structure).
Details
Redox score ?
84
PDB code
1lot
Structure name
crystal structure of the complex of actin with vitamin d-binding protein
Structure deposition date
2002-05-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
145
Residue number B
190
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 145 of Vitamin D-binding protein
Cysteine 190 of Vitamin D-binding protein
1kxp D 286 D 300
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 286 and 300.
Details
Redox score ?
84
PDB code
1kxp
Structure name
crystal structure of human vitamin d-binding protein in complex with skeletal actin
Structure deposition date
2002-02-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
286
Residue number B
300
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 286 of Vitamin D-binding protein
Cysteine 300 of Vitamin D-binding protein
1kw2 A 96 A 112
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 96 and 112.
Details
Redox score ?
84
PDB code
1kw2
Structure name
crystal structure of uncomplexed vitamin d-binding protein
Structure deposition date
2002-01-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
96
Residue number B
112
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 96 of Vitamin D-binding protein
Cysteine 112 of Vitamin D-binding protein
1j7e B 249 B 257
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 265 and 273 (249 and 257 respectively in this structure).
Details
Redox score ?
83
PDB code
1j7e
Structure name
a structural basis for the unique binding features of the human vitamin d-binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
265
Residue number B
273
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 265 of Vitamin D-binding protein
Cysteine 273 of Vitamin D-binding protein
1j78 B 436 B 446
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 452 and 462 (436 and 446 respectively in this structure).
Details
Redox score ?
82
PDB code
1j78
Structure name
crystallographic analysis of the human vitamin d binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
452
Residue number B
462
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 452 of Vitamin D-binding protein
Cysteine 462 of Vitamin D-binding protein
1kxp D 220 D 266
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 220 and 266.
Details
Redox score ?
82
PDB code
1kxp
Structure name
crystal structure of human vitamin d-binding protein in complex with skeletal actin
Structure deposition date
2002-02-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
220
Residue number B
266
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 220 of Vitamin D-binding protein
Cysteine 266 of Vitamin D-binding protein
1j7e A 391 A 437
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 407 and 453 (391 and 437 respectively in this structure).
Details
Redox score ?
82
PDB code
1j7e
Structure name
a structural basis for the unique binding features of the human vitamin d-binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
407
Residue number B
453
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 407 of Vitamin D-binding protein
Cysteine 453 of Vitamin D-binding protein
1lot A 359 A 368
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 375 and 384 (359 and 368 respectively in this structure).
Details
Redox score ?
81
PDB code
1lot
Structure name
crystal structure of the complex of actin with vitamin d-binding protein
Structure deposition date
2002-05-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
4
Peptide accession
P02774
Residue number A
375
Residue number B
384
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 375 of Vitamin D-binding protein
Cysteine 384 of Vitamin D-binding protein
1ma9 A 283 A 295
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 299 and 311 (283 and 295 respectively in this structure).
Details
Redox score ?
81
PDB code
1ma9
Structure name
crystal structure of the complex of human vitamin d binding protein and rabbit muscle actin
Structure deposition date
2002-08-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
299
Residue number B
311
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 299 of Vitamin D-binding protein
Cysteine 311 of Vitamin D-binding protein
1j7e B 95 B 96
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 111 and 112 (95 and 96 respectively in this structure).
Details
Redox score ?
64
PDB code
1j7e
Structure name
a structural basis for the unique binding features of the human vitamin d-binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
111
Residue number B
112
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 111 of Vitamin D-binding protein
Cysteine 112 of Vitamin D-binding protein
1ma9 A 359 A 360
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 375 and 376 (359 and 360 respectively in this structure).
Details
Redox score ?
62
PDB code
1ma9
Structure name
crystal structure of the complex of human vitamin d binding protein and rabbit muscle actin
Structure deposition date
2002-08-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide accession
P02774
Residue number A
375
Residue number B
376
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 375 of Vitamin D-binding protein
Cysteine 376 of Vitamin D-binding protein
1j78 A 13 A 58
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 29 and 74 (13 and 58 respectively in this structure).
Details
Redox score ?
62
PDB code
1j78
Structure name
crystallographic analysis of the human vitamin d binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
nan
Peptide accession
P02774
Residue number A
29
Residue number B
74
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 29 of Vitamin D-binding protein
Cysteine 74 of Vitamin D-binding protein
1j7e A 58 A 59
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 74 and 75 (58 and 59 respectively in this structure).
Details
Redox score ?
60
PDB code
1j7e
Structure name
a structural basis for the unique binding features of the human vitamin d-binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide accession
P02774
Residue number A
74
Residue number B
75
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 74 of Vitamin D-binding protein
Cysteine 75 of Vitamin D-binding protein
1j78 B 249 B 250
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 265 and 266 (249 and 250 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
1j78
Structure name
crystallographic analysis of the human vitamin d binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
265
Residue number B
266
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 265 of Vitamin D-binding protein
Cysteine 266 of Vitamin D-binding protein
1kw2 A 189 A 190
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 189 and 190. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
1kw2
Structure name
crystal structure of uncomplexed vitamin d-binding protein
Structure deposition date
2002-01-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
189
Residue number B
190
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 189 of Vitamin D-binding protein
Cysteine 190 of Vitamin D-binding protein
1lot A 283 A 284
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 299 and 300 (283 and 284 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
1lot
Structure name
crystal structure of the complex of actin with vitamin d-binding protein
Structure deposition date
2002-05-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
299
Residue number B
300
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 299 of Vitamin D-binding protein
Cysteine 300 of Vitamin D-binding protein
1j78 A 80 A 95
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 96 and 111 (80 and 95 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
1j78
Structure name
crystallographic analysis of the human vitamin d binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
96
Residue number B
111
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 96 of Vitamin D-binding protein
Cysteine 111 of Vitamin D-binding protein
1kxp D 452 D 453
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 452 and 453. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
1kxp
Structure name
crystal structure of human vitamin d-binding protein in complex with skeletal actin
Structure deposition date
2002-02-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
452
Residue number B
453
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 452 of Vitamin D-binding protein
Cysteine 453 of Vitamin D-binding protein
1j78 A 129 A 173
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 145 and 189 (129 and 173 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
1j78
Structure name
crystallographic analysis of the human vitamin d binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
145
Residue number B
189
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 145 of Vitamin D-binding protein
Cysteine 189 of Vitamin D-binding protein
1kxp D 300 D 311
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 300 and 311. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1kxp
Structure name
crystal structure of human vitamin d-binding protein in complex with skeletal actin
Structure deposition date
2002-02-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
300
Residue number B
311
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 300 of Vitamin D-binding protein
Cysteine 311 of Vitamin D-binding protein
1lot A 59 A 67
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 75 and 83 (59 and 67 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1lot
Structure name
crystal structure of the complex of actin with vitamin d-binding protein
Structure deposition date
2002-05-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
75
Residue number B
83
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 75 of Vitamin D-binding protein
Cysteine 83 of Vitamin D-binding protein
1lot A 270 A 283
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 286 and 299 (270 and 283 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1lot
Structure name
crystal structure of the complex of actin with vitamin d-binding protein
Structure deposition date
2002-05-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
286
Residue number B
299
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 286 of Vitamin D-binding protein
Cysteine 299 of Vitamin D-binding protein
1ma9 A 391 A 436
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 407 and 452 (391 and 436 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1ma9
Structure name
crystal structure of the complex of human vitamin d binding protein and rabbit muscle actin
Structure deposition date
2002-08-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
407
Residue number B
452
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 407 of Vitamin D-binding protein
Cysteine 452 of Vitamin D-binding protein
1j78 A 174 A 182
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 190 and 198 (174 and 182 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1j78
Structure name
crystallographic analysis of the human vitamin d binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
190
Residue number B
198
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 190 of Vitamin D-binding protein
Cysteine 198 of Vitamin D-binding protein
1j78 A 360 A 368
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 376 and 384 (360 and 368 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
1j78
Structure name
crystallographic analysis of the human vitamin d binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
376
Residue number B
384
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 376 of Vitamin D-binding protein
Cysteine 384 of Vitamin D-binding protein
1kw2 A 29 A 83
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 29 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
1kw2
Structure name
crystal structure of uncomplexed vitamin d-binding protein
Structure deposition date
2002-01-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
29
Residue number B
83
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 29 of Vitamin D-binding protein
Cysteine 83 of Vitamin D-binding protein
1j78 A 204 A 249
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 220 and 265 (204 and 249 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
1j78
Structure name
crystallographic analysis of the human vitamin d binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
220
Residue number B
265
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 220 of Vitamin D-binding protein
Cysteine 265 of Vitamin D-binding protein
1kw2 A 335 A 375
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 335 and 375. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1kw2
Structure name
crystal structure of uncomplexed vitamin d-binding protein
Structure deposition date
2002-01-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
335
Residue number B
375
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 335 of Vitamin D-binding protein
Cysteine 375 of Vitamin D-binding protein
1lot A 437 A 446
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 453 and 462 (437 and 446 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1lot
Structure name
crystal structure of the complex of actin with vitamin d-binding protein
Structure deposition date
2002-05-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
453
Residue number B
462
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 453 of Vitamin D-binding protein
Cysteine 462 of Vitamin D-binding protein
1kxp D 286 D 311
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 286 and 311. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1kxp
Structure name
crystal structure of human vitamin d-binding protein in complex with skeletal actin
Structure deposition date
2002-02-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
286
Residue number B
311
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 286 of Vitamin D-binding protein
Cysteine 311 of Vitamin D-binding protein
1kw2 A 407 A 462
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 407 and 462. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1kw2
Structure name
crystal structure of uncomplexed vitamin d-binding protein
Structure deposition date
2002-01-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
407
Residue number B
462
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 407 of Vitamin D-binding protein
Cysteine 462 of Vitamin D-binding protein
1j78 B 204 B 257
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 220 and 273 (204 and 257 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1j78
Structure name
crystallographic analysis of the human vitamin d binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
220
Residue number B
273
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 220 of Vitamin D-binding protein
Cysteine 273 of Vitamin D-binding protein
1j7e A 319 A 368
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 335 and 384 (319 and 368 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1j7e
Structure name
a structural basis for the unique binding features of the human vitamin d-binding protein
Structure deposition date
2001-05-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
335
Residue number B
384
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 335 of Vitamin D-binding protein
Cysteine 384 of Vitamin D-binding protein
1kw2 A 96 A 122
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 96 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1kw2
Structure name
crystal structure of uncomplexed vitamin d-binding protein
Structure deposition date
2002-01-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
96
Residue number B
122
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 96 of Vitamin D-binding protein
Cysteine 122 of Vitamin D-binding protein
1kw2 B 112 B 122
A redox-regulated disulphide may form within Vitamin D-binding protein between cysteines 112 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
1kw2
Structure name
crystal structure of uncomplexed vitamin d-binding protein
Structure deposition date
2002-01-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02774
Residue number A
112
Residue number B
122
Peptide name
Vitamin D-binding protein
Ligandability
Cysteine 112 of Vitamin D-binding protein
Cysteine 122 of Vitamin D-binding protein
If this tool was useful for finding a disulphide, please cite: