Complement factor H
Intermolecular
Cysteine 1218 and cysteine 1218
Intramolecular
Cysteine 21 and cysteine 66
Cysteine 901 and cysteine 926
Cysteine 477 and cysteine 505
Cysteine 237 and cysteine 262
Cysteine 178 and cysteine 205
Cysteine 870 and cysteine 915
Cysteine 569 and cysteine 611
Cysteine 52 and cysteine 80
Cysteine 1048 and cysteine 1091
More...Cysteine 931 and cysteine 973
Cysteine 416 and cysteine 442
Cysteine 114 and cysteine 141
Cysteine 781 and cysteine 803
Cysteine 597 and cysteine 623
Cysteine 1201 and cysteine 1228
Cysteine 448 and cysteine 494
Cysteine 1109 and cysteine 1152
Cysteine 959 and cysteine 984
Cysteine 630 and cysteine 673
Cysteine 719 and cysteine 744
Cysteine 659 and cysteine 684
Cysteine 1077 and cysteine 1102
Cysteine 753 and cysteine 792
Cysteine 691 and cysteine 733
Cysteine 325 and cysteine 374
Cysteine 210 and cysteine 251
Cysteine 509 and cysteine 553
Cysteine 536 and cysteine 564
Cysteine 389 and cysteine 431
Cysteine 1167 and cysteine 1218
Cysteine 1138 and cysteine 1163
Cysteine 85 and cysteine 129
Cysteine 146 and cysteine 192
Cysteine 357 and cysteine 385
5wtb E 1218 F 1218
A redox-regulated disulphide may form between two units of Complement factor H at cysteines 1218 and 1218. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5wtb
Structure name
complex structure of staphylococcus aureus sdre with human complement factor h
Structure deposition date
2016-12-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
20
Peptide A name
Complement factor H
Peptide B name
Complement factor H
Peptide A accession
P08603
Peptide B accession
P08603
Peptide A residue number
1218
Peptide B residue number
1218
Ligandability
2wii C 3 C 48
A redox-regulated disulphide may form within Complement factor H between cysteines 21 and 66 (3 and 48 respectively in this structure).
Details
Redox score ?
90
PDB code
2wii
Structure name
complement c3b in complex with factor h domains 1-4
Structure deposition date
2009-05-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
21
Residue number B
66
Peptide name
Complement factor H
Ligandability
Cysteine 21 of Complement factor H
Cysteine 66 of Complement factor H
1hfi A 36 A 61
A redox-regulated disulphide may form within Complement factor H between cysteines 901 and 926 (36 and 61 respectively in this structure).
Details
Redox score ?
89
PDB code
1hfi
Structure name
solution structure of a pair of complement modules by nuclear magnetic resonance
Structure deposition date
1993-02-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
901
Residue number B
926
Peptide name
Complement factor H
Ligandability
Cysteine 901 of Complement factor H
Cysteine 926 of Complement factor H
2uwn A 477 A 505
A redox-regulated disulphide may form within Complement factor H between cysteines 477 and 505.
Details
Redox score ?
88
PDB code
2uwn
Structure name
crystal structure of human complement factor h, scr domains 6-8 (h402 risk variant), in complex with ligand
Structure deposition date
2007-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
477
Residue number B
505
Peptide name
Complement factor H
Ligandability
Cysteine 477 of Complement factor H
Cysteine 505 of Complement factor H
2wii C 219 C 244
A redox-regulated disulphide may form within Complement factor H between cysteines 237 and 262 (219 and 244 respectively in this structure).
Details
Redox score ?
88
PDB code
2wii
Structure name
complement c3b in complex with factor h domains 1-4
Structure deposition date
2009-05-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
237
Residue number B
262
Peptide name
Complement factor H
Ligandability
Cysteine 237 of Complement factor H
Cysteine 262 of Complement factor H
5o32 G 178 G 205
A redox-regulated disulphide may form within Complement factor H between cysteines 178 and 205.
Details
Redox score ?
88
PDB code
5o32
Structure name
the structure of complement complex
Structure deposition date
2017-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
178
Residue number B
205
Peptide name
Complement factor H
Ligandability
Cysteine 178 of Complement factor H
Cysteine 205 of Complement factor H
1hfh A 5 A 50
A redox-regulated disulphide may form within Complement factor H between cysteines 870 and 915 (5 and 50 respectively in this structure).
Details
Redox score ?
87
PDB code
1hfh
Structure name
solution structure of a pair of complement modules by nuclear magnetic resonance
Structure deposition date
1993-02-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
870
Residue number B
915
Peptide name
Complement factor H
Ligandability
Cysteine 870 of Complement factor H
Cysteine 915 of Complement factor H
4b2r A 569 A 611
A redox-regulated disulphide may form within Complement factor H between cysteines 569 and 611.
Details
Redox score ?
87
PDB code
4b2r
Structure name
solution structure of ccp modules 10-11 of complement factor h
Structure deposition date
2012-07-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
569
Residue number B
611
Peptide name
Complement factor H
Ligandability
Cysteine 569 of Complement factor H
Cysteine 611 of Complement factor H
2wii C 34 C 62
A redox-regulated disulphide may form within Complement factor H between cysteines 52 and 80 (34 and 62 respectively in this structure).
Details
Redox score ?
87
PDB code
2wii
Structure name
complement c3b in complex with factor h domains 1-4
Structure deposition date
2009-05-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
52
Residue number B
80
Peptide name
Complement factor H
Ligandability
Cysteine 52 of Complement factor H
Cysteine 80 of Complement factor H
3sw0 X 1048 X 1091
A redox-regulated disulphide may form within Complement factor H between cysteines 1048 and 1091.
Details
Redox score ?
87
PDB code
3sw0
Structure name
structure of the c-terminal region (modules 18-20) of complement regulator factor h
Structure deposition date
2011-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
1048
Residue number B
1091
Peptide name
Complement factor H
Ligandability
Cysteine 1048 of Complement factor H
Cysteine 1091 of Complement factor H
1hfh A 66 A 108
A redox-regulated disulphide may form within Complement factor H between cysteines 931 and 973 (66 and 108 respectively in this structure).
Details
Redox score ?
87
PDB code
1hfh
Structure name
solution structure of a pair of complement modules by nuclear magnetic resonance
Structure deposition date
1993-02-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
931
Residue number B
973
Peptide name
Complement factor H
Ligandability
Cysteine 931 of Complement factor H
Cysteine 973 of Complement factor H
2v8e A 416 A 442
A redox-regulated disulphide may form within Complement factor H between cysteines 416 and 442.
Details
Redox score ?
87
PDB code
2v8e
Structure name
crystal structure of human complement factor h, scr domains 6-8 (h402 risk variant), in complex with ligand
Structure deposition date
2007-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
416
Residue number B
442
Peptide name
Complement factor H
Ligandability
Cysteine 416 of Complement factor H
Cysteine 442 of Complement factor H
5o32 G 114 G 141
A redox-regulated disulphide may form within Complement factor H between cysteines 114 and 141.
Details
Redox score ?
87
PDB code
5o32
Structure name
the structure of complement complex
Structure deposition date
2017-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
114
Residue number B
141
Peptide name
Complement factor H
Ligandability
Cysteine 114 of Complement factor H
Cysteine 141 of Complement factor H
2kms A 781 A 803
A redox-regulated disulphide may form within Complement factor H between cysteines 781 and 803.
Details
Redox score ?
87
PDB code
2kms
Structure name
combined high- and low-resolution techniques reveal compact structure in central portion of factor h despite long inter-modular linkers
Structure deposition date
2009-08-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
781
Residue number B
803
Peptide name
Complement factor H
Ligandability
Cysteine 781 of Complement factor H
Cysteine 803 of Complement factor H
4b2r A 597 A 623
A redox-regulated disulphide may form within Complement factor H between cysteines 597 and 623.
Details
Redox score ?
86
PDB code
4b2r
Structure name
solution structure of ccp modules 10-11 of complement factor h
Structure deposition date
2012-07-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
597
Residue number B
623
Peptide name
Complement factor H
Ligandability
Cysteine 597 of Complement factor H
Cysteine 623 of Complement factor H
5o35 C 1201 C 1228
A redox-regulated disulphide may form within Complement factor H between cysteines 1201 and 1228.
Details
Redox score ?
86
PDB code
5o35
Structure name
structure of complement proteins complex
Structure deposition date
2017-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
1201
Residue number B
1228
Peptide name
Complement factor H
Ligandability
Cysteine 1201 of Complement factor H
Cysteine 1228 of Complement factor H
2v8e A 448 A 494
A redox-regulated disulphide may form within Complement factor H between cysteines 448 and 494.
Details
Redox score ?
86
PDB code
2v8e
Structure name
crystal structure of human complement factor h, scr domains 6-8 (h402 risk variant), in complex with ligand
Structure deposition date
2007-08-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
448
Residue number B
494
Peptide name
Complement factor H
Ligandability
Cysteine 448 of Complement factor H
Cysteine 494 of Complement factor H
4ont E 1109 E 1152
A redox-regulated disulphide may form within Complement factor H between cysteines 1109 and 1152.
Details
Redox score ?
86
PDB code
4ont
Structure name
ternary host recognition complex of complement factor h, c3d, and sialic acid
Structure deposition date
2014-01-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
1109
Residue number B
1152
Peptide name
Complement factor H
Ligandability
Cysteine 1109 of Complement factor H
Cysteine 1152 of Complement factor H
1hfh A 94 A 119
A redox-regulated disulphide may form within Complement factor H between cysteines 959 and 984 (94 and 119 respectively in this structure).
Details
Redox score ?
86
PDB code
1hfh
Structure name
solution structure of a pair of complement modules by nuclear magnetic resonance
Structure deposition date
1993-02-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
959
Residue number B
984
Peptide name
Complement factor H
Ligandability
Cysteine 959 of Complement factor H
Cysteine 984 of Complement factor H
4b2s A 630 A 673
A redox-regulated disulphide may form within Complement factor H between cysteines 630 and 673.
Details
Redox score ?
86
PDB code
4b2s
Structure name
solution structure of ccp modules 11-12 of complement factor h
Structure deposition date
2012-07-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
630
Residue number B
673
Peptide name
Complement factor H
Ligandability
Cysteine 630 of Complement factor H
Cysteine 673 of Complement factor H
2kms A 719 A 744
A redox-regulated disulphide may form within Complement factor H between cysteines 719 and 744.
Details
Redox score ?
86
PDB code
2kms
Structure name
combined high- and low-resolution techniques reveal compact structure in central portion of factor h despite long inter-modular linkers
Structure deposition date
2009-08-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
719
Residue number B
744
Peptide name
Complement factor H
Ligandability
Cysteine 719 of Complement factor H
Cysteine 744 of Complement factor H
4b2s A 659 A 684
A redox-regulated disulphide may form within Complement factor H between cysteines 659 and 684.
Details
Redox score ?
86
PDB code
4b2s
Structure name
solution structure of ccp modules 11-12 of complement factor h
Structure deposition date
2012-07-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
659
Residue number B
684
Peptide name
Complement factor H
Ligandability
Cysteine 659 of Complement factor H
Cysteine 684 of Complement factor H
3sw0 X 1077 X 1102
A redox-regulated disulphide may form within Complement factor H between cysteines 1077 and 1102.
Details
Redox score ?
86
PDB code
3sw0
Structure name
structure of the c-terminal region (modules 18-20) of complement regulator factor h
Structure deposition date
2011-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
1077
Residue number B
1102
Peptide name
Complement factor H
Ligandability
Cysteine 1077 of Complement factor H
Cysteine 1102 of Complement factor H
2kms A 753 A 792
A redox-regulated disulphide may form within Complement factor H between cysteines 753 and 792.
Details
Redox score ?
85
PDB code
2kms
Structure name
combined high- and low-resolution techniques reveal compact structure in central portion of factor h despite long inter-modular linkers
Structure deposition date
2009-08-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
753
Residue number B
792
Peptide name
Complement factor H
Ligandability
Cysteine 753 of Complement factor H
Cysteine 792 of Complement factor H
4b2s A 691 A 733
A redox-regulated disulphide may form within Complement factor H between cysteines 691 and 733.
Details
Redox score ?
85
PDB code
4b2s
Structure name
solution structure of ccp modules 11-12 of complement factor h
Structure deposition date
2012-07-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
691
Residue number B
733
Peptide name
Complement factor H
Ligandability
Cysteine 691 of Complement factor H
Cysteine 733 of Complement factor H
2w81 B 325 B 374
A redox-regulated disulphide may form within Complement factor H between cysteines 325 and 374.
Details
Redox score ?
85
PDB code
2w81
Structure name
structure of a complex between neisseria meningitidis factor h binding protein and ccps 6-7 of human complement factor h
Structure deposition date
2009-01-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
325
Residue number B
374
Peptide name
Complement factor H
Ligandability
Cysteine 325 of Complement factor H
Cysteine 374 of Complement factor H
5o35 C 210 C 251
A redox-regulated disulphide may form within Complement factor H between cysteines 210 and 251.
Details
Redox score ?
85
PDB code
5o35
Structure name
structure of complement proteins complex
Structure deposition date
2017-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
210
Residue number B
251
Peptide name
Complement factor H
Ligandability
Cysteine 210 of Complement factor H
Cysteine 251 of Complement factor H
4k12 A 5 A 49
A redox-regulated disulphide may form within Complement factor H between cysteines 509 and 553 (5 and 49 respectively in this structure).
Details
Redox score ?
85
PDB code
4k12
Structure name
structural basis for host specificity of factor h binding by streptococcus pneumoniae
Structure deposition date
2013-04-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
509
Residue number B
553
Peptide name
Complement factor H
Ligandability
Cysteine 509 of Complement factor H
Cysteine 553 of Complement factor H
4k12 A 32 A 60
A redox-regulated disulphide may form within Complement factor H between cysteines 536 and 564 (32 and 60 respectively in this structure).
Details
Redox score ?
85
PDB code
4k12
Structure name
structural basis for host specificity of factor h binding by streptococcus pneumoniae
Structure deposition date
2013-04-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
536
Residue number B
564
Peptide name
Complement factor H
Ligandability
Cysteine 536 of Complement factor H
Cysteine 564 of Complement factor H
4ayd B 389 B 431
A redox-regulated disulphide may form within Complement factor H between cysteines 389 and 431.
Details
Redox score ?
84
PDB code
4ayd
Structure name
structure of a complex between ccps 6 and 7 of human complement factor h and neisseria meningitidis fhbp variant 1 r106a mutant
Structure deposition date
2012-06-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
389
Residue number B
431
Peptide name
Complement factor H
Ligandability
Cysteine 389 of Complement factor H
Cysteine 431 of Complement factor H
5nbq F 1167 F 1218
A redox-regulated disulphide may form within Complement factor H between cysteines 1167 and 1218.
Details
Redox score ?
84
PDB code
5nbq
Structure name
the structure of the tripartite complex between ospe, the c-terminal domains of factor h and c3dg
Structure deposition date
2017-03-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
1167
Residue number B
1218
Peptide name
Complement factor H
Ligandability
Cysteine 1167 of Complement factor H
Cysteine 1218 of Complement factor H
5o32 G 1138 G 1163
A redox-regulated disulphide may form within Complement factor H between cysteines 1138 and 1163.
Details
Redox score ?
84
PDB code
5o32
Structure name
the structure of complement complex
Structure deposition date
2017-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
1138
Residue number B
1163
Peptide name
Complement factor H
Ligandability
Cysteine 1138 of Complement factor H
Cysteine 1163 of Complement factor H
5o35 C 85 C 129
A redox-regulated disulphide may form within Complement factor H between cysteines 85 and 129.
Details
Redox score ?
84
PDB code
5o35
Structure name
structure of complement proteins complex
Structure deposition date
2017-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
85
Residue number B
129
Peptide name
Complement factor H
Ligandability
Cysteine 85 of Complement factor H
Cysteine 129 of Complement factor H
5o32 G 146 G 192
A redox-regulated disulphide may form within Complement factor H between cysteines 146 and 192.
Details
Redox score ?
84
PDB code
5o32
Structure name
the structure of complement complex
Structure deposition date
2017-05-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
146
Residue number B
192
Peptide name
Complement factor H
Ligandability
Cysteine 146 of Complement factor H
Cysteine 192 of Complement factor H
2w80 G 357 G 385
A redox-regulated disulphide may form within Complement factor H between cysteines 357 and 385.
Details
Redox score ?
83
PDB code
2w80
Structure name
structure of a complex between neisseria meningitidis factor h binding protein and ccps 6-7 of human complement factor h
Structure deposition date
2009-01-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08603
Residue number A
357
Residue number B
385
Peptide name
Complement factor H
Ligandability
Cysteine 357 of Complement factor H
Cysteine 385 of Complement factor H
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