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V(D)J recombination-activating protein 1

Intermolecular
Cysteine 431 and cysteine 431
Intramolecular
Cysteine 290 and cysteine 293
Cysteine 290 and cysteine 310
Cysteine 290 and cysteine 313
Cysteine 727 and cysteine 730
Cysteine 355 and cysteine 360
Cysteine 266 and cysteine 293
Cysteine 305 and cysteine 325
Cysteine 325 and cysteine 328
Cysteine 305 and cysteine 328
More...
Cysteine 266 and cysteine 313
Cysteine 266 and cysteine 290
Cysteine 293 and cysteine 313
Cysteine 293 and cysteine 310
Cysteine 325 and cysteine 332
Cysteine 310 and cysteine 313
Cysteine 266 and cysteine 310
Cysteine 305 and cysteine 332
Cysteine 290 and cysteine 317
Cysteine 328 and cysteine 332
Cysteine 651 and cysteine 652
Cysteine 313 and cysteine 317
Cysteine 897 and cysteine 902
Cysteine 317 and cysteine 325
Cysteine 317 and cysteine 332
Cysteine 902 and cysteine 907
Cysteine 293 and cysteine 317
Cysteine 599 and cysteine 652
Cysteine 467 and cysteine 478
Cysteine 599 and cysteine 656
Cysteine 727 and cysteine 796
A redox-regulated disulphide may form between two units of V(D)J recombination-activating protein 1 at cysteines 431 and 431. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4wwx
Structure name
crystal structure of the core rag1/2 recombinase
Structure deposition date
2014-11-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
88
Peptide A name
V(D)J recombination-activating protein 1
Peptide B name
V(D)J recombination-activating protein 1
Peptide A accession
P15919
Peptide B accession
P15919
Peptide A residue number
431
Peptide B residue number
431

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 290 and 293 (26 and 29 respectively in this structure).

Details

Redox score ?
91
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
2
% buried
40
Peptide accession
P15919
Residue number A
290
Residue number B
293
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 290 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 293 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 290 and 310 (26 and 46 respectively in this structure).

Details

Redox score ?
89
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
2
% buried
49
Peptide accession
P15919
Residue number A
290
Residue number B
310
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 290 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 310 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 290 and 313 (26 and 49 respectively in this structure).

Details

Redox score ?
87
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
2
% buried
40
Peptide accession
P15919
Residue number A
290
Residue number B
313
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 290 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 313 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 727 and 730.

Details

Redox score ?
86
PDB code
6oen
Structure name
cryo-em structure of mouse rag1/2 prc complex (dna1)
Structure deposition date
2019-03-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
5
% buried
72
Peptide accession
P15919
Residue number A
727
Residue number B
730
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 727 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 730 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 355 and 360 (91 and 96 respectively in this structure).

Details

Redox score ?
84
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
P15919
Residue number A
355
Residue number B
360
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 355 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 360 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 266 and 293 (2 and 29 respectively in this structure).

Details

Redox score ?
83
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
14
Peptide accession
P15919
Residue number A
266
Residue number B
293
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 266 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 293 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 305 and 325 (41 and 61 respectively in this structure).

Details

Redox score ?
82
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
20
Peptide accession
P15919
Residue number A
305
Residue number B
325
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 305 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 325 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 325 and 328 (61 and 64 respectively in this structure).

Details

Redox score ?
82
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
14
Peptide accession
P15919
Residue number A
325
Residue number B
328
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 325 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 328 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 305 and 328 (41 and 64 respectively in this structure).

Details

Redox score ?
81
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
6
Peptide accession
P15919
Residue number A
305
Residue number B
328
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 305 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 328 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 266 and 313 (2 and 49 respectively in this structure).

Details

Redox score ?
79
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
14
Peptide accession
P15919
Residue number A
266
Residue number B
313
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 266 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 313 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 266 and 290 (2 and 26 respectively in this structure).

Details

Redox score ?
77
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
2
% buried
25
Peptide accession
P15919
Residue number A
266
Residue number B
290
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 266 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 290 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 293 and 313 (29 and 49 respectively in this structure).

Details

Redox score ?
74
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
29
Peptide accession
P15919
Residue number A
293
Residue number B
313
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 293 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 313 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 293 and 310 (29 and 46 respectively in this structure).

Details

Redox score ?
74
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
38
Peptide accession
P15919
Residue number A
293
Residue number B
310
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 293 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 310 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 325 and 332 (61 and 68 respectively in this structure).

Details

Redox score ?
73
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
26
Peptide accession
P15919
Residue number A
325
Residue number B
332
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 325 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 332 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 310 and 313 (46 and 49 respectively in this structure).

Details

Redox score ?
69
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
38
Peptide accession
P15919
Residue number A
310
Residue number B
313
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 310 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 313 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 266 and 310 (2 and 46 respectively in this structure).

Details

Redox score ?
68
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
24
Peptide accession
P15919
Residue number A
266
Residue number B
310
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 266 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 310 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 305 and 332 (41 and 68 respectively in this structure).

Details

Redox score ?
67
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
17
Peptide accession
P15919
Residue number A
305
Residue number B
332
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 305 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 332 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 290 and 317 (26 and 53 respectively in this structure).

Details

Redox score ?
65
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
2
% buried
34
Peptide accession
P15919
Residue number A
290
Residue number B
317
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 290 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 317 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 328 and 332 (64 and 68 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
12
Peptide accession
P15919
Residue number A
328
Residue number B
332
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 328 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 332 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 651 and 652. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6cil
Structure name
pre-reaction complex, rag1(e962q)/2-intact/intact 12/23rss complex in mn2+
Structure deposition date
2018-02-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
79
Peptide accession
P15919
Residue number A
651
Residue number B
652
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 651 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 652 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 313 and 317 (49 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
24
Peptide accession
P15919
Residue number A
313
Residue number B
317
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 313 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 317 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 897 and 902. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
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)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
8
Peptide accession
P15919
Residue number A
897
Residue number B
902
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 897 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 902 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 317 and 325 (53 and 61 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
24
Peptide accession
P15919
Residue number A
317
Residue number B
325
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 317 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 325 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 317 and 332 (53 and 68 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
21
Peptide accession
P15919
Residue number A
317
Residue number B
332
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 317 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 332 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 902 and 907. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6cim
Structure name
pre-reaction complex, rag1(e962q)/2-nicked/intact 12/23rss complex in mn2+
Structure deposition date
2018-02-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
8
Peptide accession
P15919
Residue number A
902
Residue number B
907
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 902 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 907 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 293 and 317 (29 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1rmd
Structure name
rag1 dimerization domain
Structure deposition date
1997-01-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
24
Peptide accession
P15919
Residue number A
293
Residue number B
317
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 293 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 317 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 599 and 652. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6cim
Structure name
pre-reaction complex, rag1(e962q)/2-nicked/intact 12/23rss complex in mn2+
Structure deposition date
2018-02-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
100
Peptide accession
P15919
Residue number A
599
Residue number B
652
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 599 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 652 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 467 and 478. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6xnz
Structure name
structure of rag1 (r848m/e649v)-rag2-dna target capture complex
Structure deposition date
2020-07-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
100
Peptide accession
P15919
Residue number A
467
Residue number B
478
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 467 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 478 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 599 and 656. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
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 ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
P15919
Residue number A
599
Residue number B
656
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 599 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 656 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within V(D)J recombination-activating protein 1 between cysteines 727 and 796. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
6xny
Structure name
structure of rag1 (r848m/e649v)-rag2-dna strand transfer complex (paired-form)
Structure deposition date
2020-07-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
95
Minimum pKa ?
13
% buried
nan
Peptide accession
P15919
Residue number A
727
Residue number B
796
Peptide name
V(D)J recombination-activating protein 1

Ligandability

Cysteine 727 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 796 of V(D)J recombination-activating protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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