RelA-associated inhibitor
Intramolecular
Cysteine 709 and cysteine 744
Cysteine 734 and cysteine 744
Cysteine 669 and cysteine 699
Cysteine 669 and cysteine 703
Cysteine 703 and cysteine 744
Cysteine 709 and cysteine 734
Cysteine 699 and cysteine 703
Cysteine 699 and cysteine 709
Cysteine 703 and cysteine 709
2vge A 709 A 744
A redox-regulated disulphide may form within RelA-associated inhibitor between cysteines 709 and 744.
Details
Redox score ?
86
PDB code
2vge
Structure name
crystal structure of the c-terminal region of human iaspp
Structure deposition date
2007-11-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
3
% buried
70
Peptide accession
Q8WUF5
Residue number A
709
Residue number B
744
Peptide name
RelA-associated inhibitor
Ligandability
Cysteine 709 of RelA-associated inhibitor
Cysteine 744 of RelA-associated inhibitor
6dcx D 734 D 744
A redox-regulated disulphide may form within RelA-associated inhibitor between cysteines 734 and 744.
Details
Redox score ?
86
PDB code
6dcx
Structure name
iaspp-pp-1c structure and targeting of p53
Structure deposition date
2018-05-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
3
% buried
46
Peptide accession
Q8WUF5
Residue number A
734
Residue number B
744
Peptide name
RelA-associated inhibitor
Ligandability
Cysteine 734 of RelA-associated inhibitor
Cysteine 744 of RelA-associated inhibitor
6dcx D 669 D 699
A redox-regulated disulphide may form within RelA-associated inhibitor between cysteines 669 and 699.
Details
Redox score ?
67
PDB code
6dcx
Structure name
iaspp-pp-1c structure and targeting of p53
Structure deposition date
2018-05-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
6
% buried
62
Peptide accession
Q8WUF5
Residue number A
669
Residue number B
699
Peptide name
RelA-associated inhibitor
Ligandability
Cysteine 669 of RelA-associated inhibitor
Cysteine 699 of RelA-associated inhibitor
2vge A 669 A 703
A redox-regulated disulphide may form within RelA-associated inhibitor between cysteines 669 and 703. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
2vge
Structure name
crystal structure of the c-terminal region of human iaspp
Structure deposition date
2007-11-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
52
Peptide accession
Q8WUF5
Residue number A
669
Residue number B
703
Peptide name
RelA-associated inhibitor
Ligandability
Cysteine 669 of RelA-associated inhibitor
Cysteine 703 of RelA-associated inhibitor
2vge A 703 A 744
A redox-regulated disulphide may form within RelA-associated inhibitor between cysteines 703 and 744. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2vge
Structure name
crystal structure of the c-terminal region of human iaspp
Structure deposition date
2007-11-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
3
% buried
48
Peptide accession
Q8WUF5
Residue number A
703
Residue number B
744
Peptide name
RelA-associated inhibitor
Ligandability
Cysteine 703 of RelA-associated inhibitor
Cysteine 744 of RelA-associated inhibitor
2vge A 709 A 734
A redox-regulated disulphide may form within RelA-associated inhibitor between cysteines 709 and 734. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2vge
Structure name
crystal structure of the c-terminal region of human iaspp
Structure deposition date
2007-11-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
15
% buried
69
Peptide accession
Q8WUF5
Residue number A
709
Residue number B
734
Peptide name
RelA-associated inhibitor
Ligandability
Cysteine 709 of RelA-associated inhibitor
Cysteine 734 of RelA-associated inhibitor
6dcx C 699 C 703
A redox-regulated disulphide may form within RelA-associated inhibitor between cysteines 699 and 703. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6dcx
Structure name
iaspp-pp-1c structure and targeting of p53
Structure deposition date
2018-05-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
67
Peptide accession
Q8WUF5
Residue number A
699
Residue number B
703
Peptide name
RelA-associated inhibitor
Ligandability
Cysteine 699 of RelA-associated inhibitor
Cysteine 703 of RelA-associated inhibitor
6rz3 B 699 B 709
A redox-regulated disulphide may form within RelA-associated inhibitor between cysteines 699 and 709. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
6rz3
Structure name
crystal structure of a complex between the dna-binding domain of p53 and the carboxyl-terminal conserved region of iaspp
Structure deposition date
2019-06-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
10
% buried
86
Peptide accession
Q8WUF5
Residue number A
699
Residue number B
709
Peptide name
RelA-associated inhibitor
Ligandability
Cysteine 699 of RelA-associated inhibitor
Cysteine 709 of RelA-associated inhibitor
2vge A 703 A 709
A redox-regulated disulphide may form within RelA-associated inhibitor between cysteines 703 and 709. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
2vge
Structure name
crystal structure of the c-terminal region of human iaspp
Structure deposition date
2007-11-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
14
% buried
68
Peptide accession
Q8WUF5
Residue number A
703
Residue number B
709
Peptide name
RelA-associated inhibitor
Ligandability
Cysteine 703 of RelA-associated inhibitor
Cysteine 709 of RelA-associated inhibitor
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