Nuclear autoantigen Sp-100
Intramolecular
Cysteine 717 and cysteine 493
Cysteine 717 and cysteine 468
Cysteine 468 and cysteine 493
Cysteine 780 and cysteine 717
Cysteine 780 and cysteine 468
Cysteine 629 and cysteine 661
Cysteine 468 and cysteine 490
Cysteine 490 and cysteine 493
Cysteine 270 and cysteine 780
Cysteine 468 and cysteine 788
More...Cysteine 468 and cysteine 728
Cysteine 705 and cysteine 468
Cysteine 717 and cysteine 490
Cysteine 705 and cysteine 788
Cysteine 705 and cysteine 728
Cysteine 728 and cysteine 788
5pww A 717 A 745
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 717 and 493 (717 and 745 respectively in this structure).
Details
Redox score ?
87
PDB code
5pww
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 20)
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
22
Peptide accession
P23497
Residue number A
717
Residue number B
493
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 717 of Nuclear autoantigen Sp-100
Cysteine 493 of Nuclear autoantigen Sp-100
Cysteine 717 in protein A could not be asigned to a Uniprot residue.
5pxg B 717 B 720
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 717 and 468 (717 and 720 respectively in this structure).
Details
Redox score ?
85
PDB code
5pxg
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 40)
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
28
Peptide accession
P23497
Residue number A
717
Residue number B
468
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 717 of Nuclear autoantigen Sp-100
Cysteine 468 of Nuclear autoantigen Sp-100
Cysteine 717 in protein A could not be asigned to a Uniprot residue.
5pz0 B 720 B 745
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 468 and 493 (720 and 745 respectively in this structure).
Details
Redox score ?
81
PDB code
5pz0
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 96)
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
24
Peptide accession
P23497
Residue number A
468
Residue number B
493
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 468 of Nuclear autoantigen Sp-100
Cysteine 493 of Nuclear autoantigen Sp-100
5pze B 716 B 717
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 780 and 717 (716 and 717 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
5pze
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 110)
Structure deposition date
2017-02-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
18
Peptide accession
P23497
Residue number A
780
Residue number B
717
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 780 of Nuclear autoantigen Sp-100
Cysteine 717 of Nuclear autoantigen Sp-100
Cysteine 717 in protein B could not be asigned to a Uniprot residue.
5pzg A 716 A 720
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 780 and 468 (716 and 720 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
5pzg
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 112)
Structure deposition date
2017-02-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
16
Peptide accession
P23497
Residue number A
780
Residue number B
468
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 780 of Nuclear autoantigen Sp-100
Cysteine 468 of Nuclear autoantigen Sp-100
1h5p A 629 A 661
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 629 and 661. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1h5p
Structure name
solution structure of the human sp100b sand domain by heteronuclear nmr
Structure deposition date
2001-05-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
73
Peptide accession
P23497
Residue number A
629
Residue number B
661
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 629 of Nuclear autoantigen Sp-100
Cysteine 661 of Nuclear autoantigen Sp-100
5pxp A 720 A 742
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 468 and 490 (720 and 742 respectively in this structure).
Details
Redox score ?
nan
PDB code
5pxp
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 49)
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
38
Peptide accession
P23497
Residue number A
468
Residue number B
490
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 468 of Nuclear autoantigen Sp-100
Cysteine 490 of Nuclear autoantigen Sp-100
Uncertain whether structure cysteine 742 has been assigned to correct residue.
5pwg A 742 A 745
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 490 and 493 (742 and 745 respectively in this structure).
Details
Redox score ?
nan
PDB code
5pwg
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 3)
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
36
Peptide accession
P23497
Residue number A
490
Residue number B
493
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 490 of Nuclear autoantigen Sp-100
Cysteine 493 of Nuclear autoantigen Sp-100
Uncertain whether structure cysteine 742 has been assigned to correct residue.
5fb1 A 698 A 716
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 270 and 780 (698 and 716 respectively in this structure).
Details
Redox score ?
nan
PDB code
5fb1
Structure name
crystal structure of a phd finger bound to histone h3 k9me3 peptide
Structure deposition date
2015-12-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
32
Peptide accession
P23497
Residue number A
270
Residue number B
780
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 270 of Nuclear autoantigen Sp-100
Cysteine 780 of Nuclear autoantigen Sp-100
Uncertain whether structure cysteine 698 has been assigned to correct residue.
5pxp B 708 B 788
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 468 and 788 (708 and 788 respectively in this structure).
Details
Redox score ?
nan
PDB code
5pxp
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 49)
Structure deposition date
2017-02-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
46
Peptide accession
P23497
Residue number A
468
Residue number B
788
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 468 of Nuclear autoantigen Sp-100
Cysteine 788 of Nuclear autoantigen Sp-100
Uncertain whether structure cysteine 708 has been assigned to correct residue.
Cysteine 788 in protein B could not be asigned to a Uniprot residue.
5pxk B 708 B 728
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 468 and 728 (708 and 728 respectively in this structure).
Details
Redox score ?
nan
PDB code
5pxk
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 44)
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
31
Peptide accession
P23497
Residue number A
468
Residue number B
728
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 468 of Nuclear autoantigen Sp-100
Cysteine 728 of Nuclear autoantigen Sp-100
Uncertain whether structure cysteine 708 has been assigned to correct residue.
Cysteine 728 in protein B could not be asigned to a Uniprot residue.
5pyi A 705 A 708
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 705 and 468 (705 and 708 respectively in this structure).
Details
Redox score ?
nan
PDB code
5pyi
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 78)
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
2
% buried
36
Peptide accession
P23497
Residue number A
705
Residue number B
468
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 705 of Nuclear autoantigen Sp-100
Cysteine 468 of Nuclear autoantigen Sp-100
Cysteine 705 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 708 has been assigned to correct residue.
5pzf B 717 B 742
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 717 and 490 (717 and 742 respectively in this structure).
Details
Redox score ?
nan
PDB code
5pzf
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 111)
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
5
% buried
46
Peptide accession
P23497
Residue number A
717
Residue number B
490
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 717 of Nuclear autoantigen Sp-100
Cysteine 490 of Nuclear autoantigen Sp-100
Cysteine 717 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 742 has been assigned to correct residue.
5pwj A 705 A 788
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 705 and 788.
Details
Redox score ?
nan
PDB code
5pwj
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 6)
Structure deposition date
2017-02-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
3
% buried
60
Peptide accession
P23497
Residue number A
705
Residue number B
788
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 705 of Nuclear autoantigen Sp-100
Cysteine 788 of Nuclear autoantigen Sp-100
Cysteine 705 in protein A could not be asigned to a Uniprot residue.
Cysteine 788 in protein B could not be asigned to a Uniprot residue.
5pzj A 705 A 728
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 705 and 728.
Details
Redox score ?
nan
PDB code
5pzj
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 115)
Structure deposition date
2017-02-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
3
% buried
46
Peptide accession
P23497
Residue number A
705
Residue number B
728
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 705 of Nuclear autoantigen Sp-100
Cysteine 728 of Nuclear autoantigen Sp-100
Cysteine 705 in protein A could not be asigned to a Uniprot residue.
Cysteine 728 in protein B could not be asigned to a Uniprot residue.
5pzg A 728 A 788
A redox-regulated disulphide may form within Nuclear autoantigen Sp-100 between cysteines 728 and 788.
Details
Redox score ?
nan
PDB code
5pzg
Structure name
pandda analysis group deposition -- crystal structure of sp100 after initial refinement with no ligand modelled (structure 112)
Structure deposition date
2017-02-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
60
Peptide accession
P23497
Residue number A
728
Residue number B
788
Peptide name
Nuclear autoantigen Sp-100
Ligandability
Cysteine 728 of Nuclear autoantigen Sp-100
Cysteine 788 of Nuclear autoantigen Sp-100
Cysteine 728 in protein A could not be asigned to a Uniprot residue.
Cysteine 788 in protein B could not be asigned to a Uniprot residue.
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