BRCA1-associated RING domain protein 1
Intermolecular
Cysteine 743 and cysteine 743
Intramolecular
Cysteine 50 and cysteine 53
Cysteine 50 and cysteine 71
Cysteine 53 and cysteine 74
Cysteine 53 and cysteine 71
Cysteine 83 and cysteine 86
Cysteine 66 and cysteine 86
Cysteine 50 and cysteine 74
Cysteine 66 and cysteine 83
Cysteine 71 and cysteine 74
More...Cysteine 639 and cysteine 645
Cysteine 78 and cysteine 83
Cysteine 74 and cysteine 83
Cysteine 78 and cysteine 86
Cysteine 74 and cysteine 78
Cysteine 66 and cysteine 78
Cysteine 62 and cysteine 83
Cysteine 62 and cysteine 66
Cysteine 53 and cysteine 78
Cysteine 62 and cysteine 86
Cysteine 53 and cysteine 62
Cysteine 675 and cysteine 733
Cysteine 620 and cysteine 628
Cysteine 675 and cysteine 766
3fa2 A 743 B 743
A redox-regulated disulphide may form between two units of BRCA1-associated RING domain protein 1 at cysteines 743 and 743.
Details
Redox score ?
89
PDB code
3fa2
Structure name
crystal structure of the brca1 associated ring domain (bard1) tandem brct domains
Structure deposition date
2008-11-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide A name
BRCA1-associated RING domain protein 1
Peptide B name
BRCA1-associated RING domain protein 1
Peptide A accession
Q99728
Peptide B accession
Q99728
Peptide A residue number
743
Peptide B residue number
743
Ligandability
1jm7 B 50 B 53
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 50 and 53.
Details
Redox score ?
86
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
14
Peptide accession
Q99728
Residue number A
50
Residue number B
53
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 50 of BRCA1-associated RING domain protein 1
Cysteine 53 of BRCA1-associated RING domain protein 1
1jm7 B 50 B 71
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 50 and 71.
Details
Redox score ?
85
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
6
% buried
22
Peptide accession
Q99728
Residue number A
50
Residue number B
71
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 50 of BRCA1-associated RING domain protein 1
Cysteine 71 of BRCA1-associated RING domain protein 1
1jm7 B 53 B 74
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 53 and 74.
Details
Redox score ?
80
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
2
Peptide accession
Q99728
Residue number A
53
Residue number B
74
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 53 of BRCA1-associated RING domain protein 1
Cysteine 74 of BRCA1-associated RING domain protein 1
1jm7 B 53 B 71
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 53 and 71.
Details
Redox score ?
80
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
8
Peptide accession
Q99728
Residue number A
53
Residue number B
71
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 53 of BRCA1-associated RING domain protein 1
Cysteine 71 of BRCA1-associated RING domain protein 1
1jm7 B 83 B 86
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 83 and 86.
Details
Redox score ?
80
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
8
Peptide accession
Q99728
Residue number A
83
Residue number B
86
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 83 of BRCA1-associated RING domain protein 1
Cysteine 86 of BRCA1-associated RING domain protein 1
1jm7 B 66 B 86
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 66 and 86.
Details
Redox score ?
78
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
22
Peptide accession
Q99728
Residue number A
66
Residue number B
86
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 66 of BRCA1-associated RING domain protein 1
Cysteine 86 of BRCA1-associated RING domain protein 1
1jm7 B 50 B 74
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 50 and 74.
Details
Redox score ?
78
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
17
Peptide accession
Q99728
Residue number A
50
Residue number B
74
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 50 of BRCA1-associated RING domain protein 1
Cysteine 74 of BRCA1-associated RING domain protein 1
1jm7 B 66 B 83
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 66 and 83.
Details
Redox score ?
76
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
24
Peptide accession
Q99728
Residue number A
66
Residue number B
83
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 66 of BRCA1-associated RING domain protein 1
Cysteine 83 of BRCA1-associated RING domain protein 1
1jm7 B 71 B 74
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 71 and 74.
Details
Redox score ?
74
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
10
Peptide accession
Q99728
Residue number A
71
Residue number B
74
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 71 of BRCA1-associated RING domain protein 1
Cysteine 74 of BRCA1-associated RING domain protein 1
6m14 B 639 B 645
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 639 and 645.
Details
Redox score ?
66
PDB code
6m14
Structure name
crystal structure of the bard1 brct mutant
Structure deposition date
2020-02-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
49
Minimum pKa ?
11
% buried
42
Peptide accession
Q99728
Residue number A
639
Residue number B
645
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 639 of BRCA1-associated RING domain protein 1
Cysteine 645 of BRCA1-associated RING domain protein 1
1jm7 B 78 B 83
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 78 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
5
Peptide accession
Q99728
Residue number A
78
Residue number B
83
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 78 of BRCA1-associated RING domain protein 1
Cysteine 83 of BRCA1-associated RING domain protein 1
7jzv B 74 B 83
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 74 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
7jzv
Structure name
cryo-em structure of the brca1-ubch5c/bard1 e3-e2 module bound to a nucleosome
Structure deposition date
2020-09-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
34
Peptide accession
Q99728
Residue number A
74
Residue number B
83
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 74 of BRCA1-associated RING domain protein 1
Cysteine 83 of BRCA1-associated RING domain protein 1
1jm7 B 78 B 86
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 78 and 86. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
2
Peptide accession
Q99728
Residue number A
78
Residue number B
86
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 78 of BRCA1-associated RING domain protein 1
Cysteine 86 of BRCA1-associated RING domain protein 1
1jm7 B 74 B 78
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 74 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
2
Peptide accession
Q99728
Residue number A
74
Residue number B
78
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 74 of BRCA1-associated RING domain protein 1
Cysteine 78 of BRCA1-associated RING domain protein 1
1jm7 B 66 B 78
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 66 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
19
Peptide accession
Q99728
Residue number A
66
Residue number B
78
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 66 of BRCA1-associated RING domain protein 1
Cysteine 78 of BRCA1-associated RING domain protein 1
1jm7 B 62 B 83
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 62 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
49
Peptide accession
Q99728
Residue number A
62
Residue number B
83
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 62 of BRCA1-associated RING domain protein 1
Cysteine 83 of BRCA1-associated RING domain protein 1
1jm7 B 62 B 66
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 62 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
1jm7
Structure name
solution structure of the brca1/bard1 ring-domain heterodimer
Structure deposition date
2001-07-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
63
Peptide accession
Q99728
Residue number A
62
Residue number B
66
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 62 of BRCA1-associated RING domain protein 1
Cysteine 66 of BRCA1-associated RING domain protein 1
7jzv B 53 B 78
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 53 and 78. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
7jzv
Structure name
cryo-em structure of the brca1-ubch5c/bard1 e3-e2 module bound to a nucleosome
Structure deposition date
2020-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
36
Peptide accession
Q99728
Residue number A
53
Residue number B
78
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 53 of BRCA1-associated RING domain protein 1
Cysteine 78 of BRCA1-associated RING domain protein 1
7lyb N 62 N 86
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 62 and 86. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
7lyb
Structure name
cryo-em structure of the human nucleosome core particle in complex with brca1-bard1-ubch5c
Structure deposition date
2021-03-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
58
Peptide accession
Q99728
Residue number A
62
Residue number B
86
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 62 of BRCA1-associated RING domain protein 1
Cysteine 86 of BRCA1-associated RING domain protein 1
7jzv B 53 B 62
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 53 and 62. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
7jzv
Structure name
cryo-em structure of the brca1-ubch5c/bard1 e3-e2 module bound to a nucleosome
Structure deposition date
2020-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
57
Peptide accession
Q99728
Residue number A
53
Residue number B
62
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 53 of BRCA1-associated RING domain protein 1
Cysteine 62 of BRCA1-associated RING domain protein 1
7e8i K 675 K 733
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 675 and 733. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
7e8i
Structure name
structural insight into brca1-bard1 complex recruitment to damaged chromatin
Structure deposition date
2021-03-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
88
Peptide accession
Q99728
Residue number A
675
Residue number B
733
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 675 of BRCA1-associated RING domain protein 1
Cysteine 733 of BRCA1-associated RING domain protein 1
2nte A 620 A 628
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 620 and 628. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
2nte
Structure name
crystal structure of the bard1 brct domains
Structure deposition date
2006-11-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
87
Peptide accession
Q99728
Residue number A
620
Residue number B
628
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 620 of BRCA1-associated RING domain protein 1
Cysteine 628 of BRCA1-associated RING domain protein 1
6m14 B 675 B 766
A redox-regulated disulphide may form within BRCA1-associated RING domain protein 1 between cysteines 675 and 766. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
6m14
Structure name
crystal structure of the bard1 brct mutant
Structure deposition date
2020-02-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
100
Peptide accession
Q99728
Residue number A
675
Residue number B
766
Peptide name
BRCA1-associated RING domain protein 1
Ligandability
Cysteine 675 of BRCA1-associated RING domain protein 1
Cysteine 766 of BRCA1-associated RING domain protein 1
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