Transcription factor Sp1
Intramolecular
Cysteine 658 and cysteine 663
Cysteine 628 and cysteine 633 L
Cysteine 688 and cysteine 691
Cysteine 658 and cysteine 9
Cysteine 9 and cysteine 663
1sp2 A 5 A 10
A redox-regulated disulphide may form within Transcription factor Sp1 between cysteines 658 and 663 (5 and 10 respectively in this structure).
Details
Redox score ?
88
PDB code
1sp2
Structure name
nmr structure of a zinc finger domain from transcription factor sp1f2, minimized average structure
Structure deposition date
1996-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
0
Peptide accession
P08047
Residue number A
658
Residue number B
663
Peptide name
Transcription factor Sp1
Ligandability
Cysteine 658 of Transcription factor Sp1
Cysteine 663 of Transcription factor Sp1
1va1 A 539 A 544
A redox-regulated disulphide may form within Transcription factor Sp1 between cysteines 628 and 633 (539 and 544 respectively in this structure).
Details
Redox score ?
85
PDB code
1va1
Structure name
solution structure of transcription factor sp1 dna binding domain (zinc finger 1)
Structure deposition date
2004-02-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
8
% buried
0
Peptide accession
P08047
Residue number A
628
Residue number B
633
Peptide name
Transcription factor Sp1
Ligandability
Cysteine 628 of Transcription factor Sp1
Cysteine 633 of Transcription factor Sp1
1sp1 A 5 A 8
A redox-regulated disulphide may form within Transcription factor Sp1 between cysteines 688 and 691 (5 and 8 respectively in this structure).
Details
Redox score ?
84
PDB code
1sp1
Structure name
nmr structure of a zinc finger domain from transcription factor sp1f3, minimized average structure
Structure deposition date
1996-11-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
0
Peptide accession
P08047
Residue number A
688
Residue number B
691
Peptide name
Transcription factor Sp1
Ligandability
Cysteine 688 of Transcription factor Sp1
Cysteine 691 of Transcription factor Sp1
6uco A 5 A 9
A redox-regulated disulphide may form within Transcription factor Sp1 between cysteines 658 and 9 (5 and 9 respectively in this structure).
Details
Redox score ?
nan
PDB code
6uco
Structure name
backbone-modified variant of zinc finger 2 from the transcription factor sp1 dna binding domain: btd in the metal-binding turn
Structure deposition date
2019-09-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
0
Peptide accession
P08047
Residue number A
658
Residue number B
9
Peptide name
Transcription factor Sp1
Ligandability
Cysteine 658 of Transcription factor Sp1
Cysteine 9 of Transcription factor Sp1
Cysteine 9 in protein B could not be asigned to a Uniprot residue.
6uco A 9 A 10
A redox-regulated disulphide may form within Transcription factor Sp1 between cysteines 9 and 663 (9 and 10 respectively in this structure).
Details
Redox score ?
nan
PDB code
6uco
Structure name
backbone-modified variant of zinc finger 2 from the transcription factor sp1 dna binding domain: btd in the metal-binding turn
Structure deposition date
2019-09-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide accession
P08047
Residue number A
9
Residue number B
663
Peptide name
Transcription factor Sp1
Ligandability
Cysteine 9 of Transcription factor Sp1
Cysteine 663 of Transcription factor Sp1
Cysteine 9 in protein A could not be asigned to a Uniprot residue.
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