Complement factor B
Intramolecular
Cysteine 62 and cysteine 98
Cysteine 37 and cysteine 76
Cysteine 165 and cysteine 205
Cysteine 103 and cysteine 145
Cysteine 131 and cysteine 158
Cysteine 191 and cysteine 218
Cysteine 599 and cysteine 615
Cysteine 511 and cysteine 527
Cysteine 695 and cysteine 725
Cysteine 656 and cysteine 682
More...Cysteine 615 and cysteine 615
Cysteine 599 and cysteine 599
Cysteine 478 and cysteine 596
Cysteine 428 and cysteine 98
3hs0 D 37 D 73
A redox-regulated disulphide may form within Complement factor B between cysteines 62 and 98 (37 and 73 respectively in this structure).
Details
Redox score ?
87
PDB code
3hs0
Structure name
cobra venom factor (cvf) in complex with human factor b
Structure deposition date
2009-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
62
Residue number B
98
Peptide name
Complement factor B
Ligandability
Cysteine 62 of Complement factor B
Cysteine 98 of Complement factor B
7noz F 37 F 76
A redox-regulated disulphide may form within Complement factor B between cysteines 37 and 76.
Details
Redox score ?
87
PDB code
7noz
Structure name
structure of the nanobody stablized properdin bound alternative pathway proconvertase c3b:fb:fp
Structure deposition date
2021-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
37
Residue number B
76
Peptide name
Complement factor B
Ligandability
Cysteine 37 of Complement factor B
Cysteine 76 of Complement factor B
3hs0 D 140 D 180
A redox-regulated disulphide may form within Complement factor B between cysteines 165 and 205 (140 and 180 respectively in this structure).
Details
Redox score ?
86
PDB code
3hs0
Structure name
cobra venom factor (cvf) in complex with human factor b
Structure deposition date
2009-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
165
Residue number B
205
Peptide name
Complement factor B
Ligandability
Cysteine 165 of Complement factor B
Cysteine 205 of Complement factor B
3hs0 D 78 D 120
A redox-regulated disulphide may form within Complement factor B between cysteines 103 and 145 (78 and 120 respectively in this structure).
Details
Redox score ?
84
PDB code
3hs0
Structure name
cobra venom factor (cvf) in complex with human factor b
Structure deposition date
2009-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
103
Residue number B
145
Peptide name
Complement factor B
Ligandability
Cysteine 103 of Complement factor B
Cysteine 145 of Complement factor B
3hs0 I 106 I 133
A redox-regulated disulphide may form within Complement factor B between cysteines 131 and 158 (106 and 133 respectively in this structure).
Details
Redox score ?
84
PDB code
3hs0
Structure name
cobra venom factor (cvf) in complex with human factor b
Structure deposition date
2009-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
131
Residue number B
158
Peptide name
Complement factor B
Ligandability
Cysteine 131 of Complement factor B
Cysteine 158 of Complement factor B
7jtn A 166 A 193
A redox-regulated disulphide may form within Complement factor B between cysteines 191 and 218 (166 and 193 respectively in this structure).
Details
Redox score ?
83
PDB code
7jtn
Structure name
human complement factor b inhibited by a slow off-rate modified aptamer of 29 bases
Structure deposition date
2020-08-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
191
Residue number B
218
Peptide name
Complement factor B
Ligandability
Cysteine 191 of Complement factor B
Cysteine 218 of Complement factor B
1rrk A 574 A 590
A redox-regulated disulphide may form within Complement factor B between cysteines 599 and 615 (574 and 590 respectively in this structure).
Details
Redox score ?
83
PDB code
1rrk
Structure name
crystal structure analysis of the bb segment of factor b
Structure deposition date
2003-12-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
599
Residue number B
615
Peptide name
Complement factor B
Ligandability
Cysteine 599 of Complement factor B
Cysteine 615 of Complement factor B
6rur J 486 J 502
A redox-regulated disulphide may form within Complement factor B between cysteines 511 and 527 (486 and 502 respectively in this structure).
Details
Redox score ?
82
PDB code
6rur
Structure name
structure of the scin stabilized c3bbb convertase bound to properdin
Structure deposition date
2019-05-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
511
Residue number B
527
Peptide name
Complement factor B
Ligandability
Cysteine 511 of Complement factor B
Cysteine 527 of Complement factor B
2win J 670 J 700
A redox-regulated disulphide may form within Complement factor B between cysteines 695 and 725 (670 and 700 respectively in this structure).
Details
Redox score ?
82
PDB code
2win
Structure name
c3 convertase (c3bbb) stabilized by scin
Structure deposition date
2009-05-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
695
Residue number B
725
Peptide name
Complement factor B
Ligandability
Cysteine 695 of Complement factor B
Cysteine 725 of Complement factor B
3hrz D 631 D 657
A redox-regulated disulphide may form within Complement factor B between cysteines 656 and 682 (631 and 657 respectively in this structure).
Details
Redox score ?
80
PDB code
3hrz
Structure name
cobra venom factor (cvf) in complex with human factor b
Structure deposition date
2009-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
656
Residue number B
682
Peptide name
Complement factor B
Ligandability
Cysteine 656 of Complement factor B
Cysteine 682 of Complement factor B
1dle A 125 A 125
A redox-regulated disulphide may form within Complement factor B between cysteines 615 and 615 (125 and 125 respectively in this structure).
Details
Redox score ?
79
PDB code
1dle
Structure name
factor b serine protease domain
Structure deposition date
1999-12-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
615
Residue number B
615
Peptide name
Complement factor B
Ligandability
1dle A 125 A 125
A redox-regulated disulphide may form within Complement factor B between cysteines 599 and 599 (125 and 125 respectively in this structure).
Details
Redox score ?
79
PDB code
1dle
Structure name
factor b serine protease domain
Structure deposition date
1999-12-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
599
Residue number B
599
Peptide name
Complement factor B
Ligandability
3hs0 D 453 D 571
A redox-regulated disulphide may form within Complement factor B between cysteines 478 and 596 (453 and 571 respectively in this structure).
Details
Redox score ?
79
PDB code
3hs0
Structure name
cobra venom factor (cvf) in complex with human factor b
Structure deposition date
2009-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
478
Residue number B
596
Peptide name
Complement factor B
Ligandability
Cysteine 478 of Complement factor B
Cysteine 596 of Complement factor B
1rtk A 428 A 435
A redox-regulated disulphide may form within Complement factor B between cysteines 428 and 98 (428 and 435 respectively in this structure).
Details
Redox score ?
nan
PDB code
1rtk
Structure name
crystal structure analysis of the bb segment of factor b complexed with 4-guanidinobenzoic acid
Structure deposition date
2003-12-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00751
Residue number A
428
Residue number B
98
Peptide name
Complement factor B
Ligandability
Cysteine 428 of Complement factor B
Cysteine 98 of Complement factor B
Cysteine 428 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 435 has been assigned to correct residue.
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