V(D)J recombination-activating protein 2
Intramolecular
Cysteine 423 and cysteine 458
Cysteine 419 and cysteine 458
Cysteine 420 and cysteine 458
Cysteine 419 and cysteine 420
Cysteine 446 and cysteine 478
Cysteine 420 and cysteine 423
Cysteine 67 and cysteine 124
Cysteine 420 and cysteine 478
Cysteine 287 and cysteine 350
Cysteine 423 and cysteine 478
More...Cysteine 419 and cysteine 478
Cysteine 420 and cysteine 446
Cysteine 419 and cysteine 446
Cysteine 419 and cysteine 423
Cysteine 458 and cysteine 478
2v88 B 423 B 458
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 423 and 458.
Details
Redox score ?
93
PDB code
2v88
Structure name
crystal structure of rag2-phd finger in complex with h3r2me2sk4me2 peptide
Structure deposition date
2007-08-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
2
% buried
36
Peptide accession
P21784
Residue number A
423
Residue number B
458
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 423 of V(D)J recombination-activating protein 2
Cysteine 458 of V(D)J recombination-activating protein 2
2v83 B 419 B 458
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 419 and 458.
Details
Redox score ?
91
PDB code
2v83
Structure name
crystal structure of rag2-phd finger in complex with h3k4me3 peptide
Structure deposition date
2007-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
2
% buried
50
Peptide accession
P21784
Residue number A
419
Residue number B
458
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 419 of V(D)J recombination-activating protein 2
Cysteine 458 of V(D)J recombination-activating protein 2
2v83 B 420 B 458
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 420 and 458.
Details
Redox score ?
86
PDB code
2v83
Structure name
crystal structure of rag2-phd finger in complex with h3k4me3 peptide
Structure deposition date
2007-08-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
50
Minimum pKa ?
2
% buried
32
Peptide accession
P21784
Residue number A
420
Residue number B
458
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 420 of V(D)J recombination-activating protein 2
Cysteine 458 of V(D)J recombination-activating protein 2
2v83 A 419 A 420
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 419 and 420.
Details
Redox score ?
82
PDB code
2v83
Structure name
crystal structure of rag2-phd finger in complex with h3k4me3 peptide
Structure deposition date
2007-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
30
Peptide accession
P21784
Residue number A
419
Residue number B
420
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 419 of V(D)J recombination-activating protein 2
Cysteine 420 of V(D)J recombination-activating protein 2
2v86 B 446 B 478
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 446 and 478.
Details
Redox score ?
80
PDB code
2v86
Structure name
crystal structure of rag2-phd finger in complex with h3r2me2ak4me3 peptide
Structure deposition date
2007-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
32
Peptide accession
P21784
Residue number A
446
Residue number B
478
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 446 of V(D)J recombination-activating protein 2
Cysteine 478 of V(D)J recombination-activating protein 2
2v87 B 420 B 423
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 420 and 423.
Details
Redox score ?
76
PDB code
2v87
Structure name
crystal structure of rag2-phd finger in complex with h3r2me2sk4me3 peptide
Structure deposition date
2007-08-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
22
Peptide accession
P21784
Residue number A
420
Residue number B
423
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 420 of V(D)J recombination-activating protein 2
Cysteine 423 of V(D)J recombination-activating protein 2
6cik D 67 D 124
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 67 and 124.
Details
Redox score ?
66
PDB code
6cik
Structure name
pre-reaction complex, rag1(e962q)/2-intact/nicked 12/23rss complex in mn2+
Structure deposition date
2018-02-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
7
% buried
86
Peptide accession
P21784
Residue number A
67
Residue number B
124
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 67 of V(D)J recombination-activating protein 2
Cysteine 124 of V(D)J recombination-activating protein 2
2v86 B 420 B 478
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 420 and 478.
Details
Redox score ?
63
PDB code
2v86
Structure name
crystal structure of rag2-phd finger in complex with h3r2me2ak4me3 peptide
Structure deposition date
2007-08-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
50
Peptide accession
P21784
Residue number A
420
Residue number B
478
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 420 of V(D)J recombination-activating protein 2
Cysteine 478 of V(D)J recombination-activating protein 2
6cik B 287 B 350
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 287 and 350. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
6cik
Structure name
pre-reaction complex, rag1(e962q)/2-intact/nicked 12/23rss complex in mn2+
Structure deposition date
2018-02-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
54
Peptide accession
P21784
Residue number A
287
Residue number B
350
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 287 of V(D)J recombination-activating protein 2
Cysteine 350 of V(D)J recombination-activating protein 2
2jwo A 423 A 478
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 423 and 478. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
2jwo
Structure name
a phd finger motif in the c-terminus of rag2 modulates recombination activity
Structure deposition date
2007-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
14
Peptide accession
P21784
Residue number A
423
Residue number B
478
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 423 of V(D)J recombination-activating protein 2
Cysteine 478 of V(D)J recombination-activating protein 2
2v88 B 419 B 478
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 419 and 478. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
2v88
Structure name
crystal structure of rag2-phd finger in complex with h3r2me2sk4me2 peptide
Structure deposition date
2007-08-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
37
Peptide accession
P21784
Residue number A
419
Residue number B
478
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 419 of V(D)J recombination-activating protein 2
Cysteine 478 of V(D)J recombination-activating protein 2
2jwo A 420 A 446
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 420 and 446. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2jwo
Structure name
a phd finger motif in the c-terminus of rag2 modulates recombination activity
Structure deposition date
2007-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
8
Peptide accession
P21784
Residue number A
420
Residue number B
446
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 420 of V(D)J recombination-activating protein 2
Cysteine 446 of V(D)J recombination-activating protein 2
2jwo A 419 A 446
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 419 and 446. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2jwo
Structure name
a phd finger motif in the c-terminus of rag2 modulates recombination activity
Structure deposition date
2007-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
20
Peptide accession
P21784
Residue number A
419
Residue number B
446
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 419 of V(D)J recombination-activating protein 2
Cysteine 446 of V(D)J recombination-activating protein 2
2v86 B 419 B 423
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 419 and 423. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2v86
Structure name
crystal structure of rag2-phd finger in complex with h3r2me2ak4me3 peptide
Structure deposition date
2007-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
23
% buried
nan
Peptide accession
P21784
Residue number A
419
Residue number B
423
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 419 of V(D)J recombination-activating protein 2
Cysteine 423 of V(D)J recombination-activating protein 2
2jwo A 458 A 478
A redox-regulated disulphide may form within V(D)J recombination-activating protein 2 between cysteines 458 and 478. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2jwo
Structure name
a phd finger motif in the c-terminus of rag2 modulates recombination activity
Structure deposition date
2007-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
24
Peptide accession
P21784
Residue number A
458
Residue number B
478
Peptide name
V(D)J recombination-activating protein 2
Ligandability
Cysteine 458 of V(D)J recombination-activating protein 2
Cysteine 478 of V(D)J recombination-activating protein 2
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