Neurofibromin
Intramolecular
Cysteine 379 and cysteine 383
Cysteine 324 and cysteine 328
Cysteine 1930 and cysteine 1945
Cysteine 328 and cysteine 383
Cysteine 1878 and cysteine 1882
Cysteine 714 and cysteine 721
Cysteine 2216 and cysteine 2223
Cysteine 383 and cysteine 397
Cysteine 324 and cysteine 379
Cysteine 2134 and cysteine 2136
More...Cysteine 187 and cysteine 245
Cysteine 324 and cysteine 383
Cysteine 1792 and cysteine 1817
Cysteine 1117 and cysteine 1144
Cysteine 2134 and cysteine 2216
Cysteine 2136 and cysteine 2216
Cysteine 434 and cysteine 509
Cysteine 328 and cysteine 379
Cysteine 245 and cysteine 277
Cysteine 582 and cysteine 709
Cysteine 709 and cysteine 714
Cysteine 379 and cysteine 397
Cysteine 1288 and cysteine 1367
Cysteine 1288 and cysteine 1365
Cysteine 1365 and cysteine 1367
7pgs F 379 F 383
A redox-regulated disulphide may form within Neurofibromin between cysteines 379 and 383.
Details
Redox score ?
74
PDB code
7pgs
Structure name
consensus structure of human neurofibromin isoform 2
Structure deposition date
2021-08-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
7
% buried
96
Peptide accession
P21359
Residue number A
379
Residue number B
383
Peptide name
Neurofibromin
Ligandability
Cysteine 379 of Neurofibromin
Cysteine 383 of Neurofibromin
7pgs F 324 F 328
A redox-regulated disulphide may form within Neurofibromin between cysteines 324 and 328.
Details
Redox score ?
66
PDB code
7pgs
Structure name
consensus structure of human neurofibromin isoform 2
Structure deposition date
2021-08-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
8
% buried
94
Peptide accession
P21359
Residue number A
324
Residue number B
328
Peptide name
Neurofibromin
Ligandability
Cysteine 324 of Neurofibromin
Cysteine 328 of Neurofibromin
7pgr F 1930 F 1945
A redox-regulated disulphide may form within Neurofibromin between cysteines 1930 and 1945. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
7pgr
Structure name
the structure of human neurofibromin isoform 2 in closed conformation
Structure deposition date
2021-08-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
96
Peptide accession
P21359
Residue number A
1930
Residue number B
1945
Peptide name
Neurofibromin
Ligandability
Cysteine 1930 of Neurofibromin
Cysteine 1945 of Neurofibromin
7r04 B 328 B 383
A redox-regulated disulphide may form within Neurofibromin between cysteines 328 and 383. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
7r04
Structure name
neurofibromin in open conformation
Structure deposition date
2022-02-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
92
Peptide accession
P21359
Residue number A
328
Residue number B
383
Peptide name
Neurofibromin
Ligandability
Cysteine 328 of Neurofibromin
Cysteine 383 of Neurofibromin
7pgs N 1878 N 1882
A redox-regulated disulphide may form within Neurofibromin between cysteines 1878 and 1882. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
7pgs
Structure name
consensus structure of human neurofibromin isoform 2
Structure deposition date
2021-08-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
44
Peptide accession
P21359
Residue number A
1878
Residue number B
1882
Peptide name
Neurofibromin
Ligandability
Cysteine 1878 of Neurofibromin
Cysteine 1882 of Neurofibromin
7r04 B 714 B 721
A redox-regulated disulphide may form within Neurofibromin between cysteines 714 and 721. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7r04
Structure name
neurofibromin in open conformation
Structure deposition date
2022-02-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
17
Peptide accession
P21359
Residue number A
714
Residue number B
721
Peptide name
Neurofibromin
Ligandability
Cysteine 714 of Neurofibromin
Cysteine 721 of Neurofibromin
7pgs F 2216 F 2223
A redox-regulated disulphide may form within Neurofibromin between cysteines 2216 and 2223. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7pgs
Structure name
consensus structure of human neurofibromin isoform 2
Structure deposition date
2021-08-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
52
Peptide accession
P21359
Residue number A
2216
Residue number B
2223
Peptide name
Neurofibromin
Ligandability
Cysteine 2216 of Neurofibromin
Cysteine 2223 of Neurofibromin
7r03 B 383 B 397
A redox-regulated disulphide may form within Neurofibromin between cysteines 383 and 397. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
7r03
Structure name
neurofibromin occluded conformation
Structure deposition date
2022-02-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
88
Peptide accession
P21359
Residue number A
383
Residue number B
397
Peptide name
Neurofibromin
Ligandability
Cysteine 383 of Neurofibromin
Cysteine 397 of Neurofibromin
7pgs F 324 F 379
A redox-regulated disulphide may form within Neurofibromin between cysteines 324 and 379. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
7pgs
Structure name
consensus structure of human neurofibromin isoform 2
Structure deposition date
2021-08-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
8
% buried
96
Peptide accession
P21359
Residue number A
324
Residue number B
379
Peptide name
Neurofibromin
Ligandability
Cysteine 324 of Neurofibromin
Cysteine 379 of Neurofibromin
7r04 B 2113 B 2115
A redox-regulated disulphide may form within Neurofibromin between cysteines 2134 and 2136 (2113 and 2115 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
7r04
Structure name
neurofibromin in open conformation
Structure deposition date
2022-02-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
82
Peptide accession
P21359
Residue number A
2134
Residue number B
2136
Peptide name
Neurofibromin
Ligandability
Cysteine 2134 of Neurofibromin
Cysteine 2136 of Neurofibromin
7pgt N 187 N 245
A redox-regulated disulphide may form within Neurofibromin between cysteines 187 and 245. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
7pgt
Structure name
the structure of human neurofibromin isoform 2 in opened conformation
Structure deposition date
2021-08-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
52
Peptide accession
P21359
Residue number A
187
Residue number B
245
Peptide name
Neurofibromin
Ligandability
Cysteine 187 of Neurofibromin
Cysteine 245 of Neurofibromin
7pgp N 324 N 383
A redox-regulated disulphide may form within Neurofibromin between cysteines 324 and 383. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7pgp
Structure name
the core structure of human neurofibromin isoform 2
Structure deposition date
2021-08-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
7
% buried
90
Peptide accession
P21359
Residue number A
324
Residue number B
383
Peptide name
Neurofibromin
Ligandability
Cysteine 324 of Neurofibromin
Cysteine 383 of Neurofibromin
7pgt N 1792 N 1817
A redox-regulated disulphide may form within Neurofibromin between cysteines 1792 and 1817. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7pgt
Structure name
the structure of human neurofibromin isoform 2 in opened conformation
Structure deposition date
2021-08-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
10
Peptide accession
P21359
Residue number A
1792
Residue number B
1817
Peptide name
Neurofibromin
Ligandability
Cysteine 1792 of Neurofibromin
Cysteine 1817 of Neurofibromin
7r03 A 1117 A 1144
A redox-regulated disulphide may form within Neurofibromin between cysteines 1117 and 1144. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
7r03
Structure name
neurofibromin occluded conformation
Structure deposition date
2022-02-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
29
Peptide accession
P21359
Residue number A
1117
Residue number B
1144
Peptide name
Neurofibromin
Ligandability
Cysteine 1117 of Neurofibromin
Cysteine 1144 of Neurofibromin
7pgu F 2134 F 2216
A redox-regulated disulphide may form within Neurofibromin between cysteines 2134 and 2216. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
7pgu
Structure name
autoinhibited structure of human neurofibromin isoform 2 stabilized by zinc
Structure deposition date
2021-08-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
78
Peptide accession
P21359
Residue number A
2134
Residue number B
2216
Peptide name
Neurofibromin
Ligandability
Cysteine 2134 of Neurofibromin
Cysteine 2216 of Neurofibromin
7pgt F 2136 F 2216
A redox-regulated disulphide may form within Neurofibromin between cysteines 2136 and 2216. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
7pgt
Structure name
the structure of human neurofibromin isoform 2 in opened conformation
Structure deposition date
2021-08-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
61
Peptide accession
P21359
Residue number A
2136
Residue number B
2216
Peptide name
Neurofibromin
Ligandability
Cysteine 2136 of Neurofibromin
Cysteine 2216 of Neurofibromin
7pgt F 434 F 509
A redox-regulated disulphide may form within Neurofibromin between cysteines 434 and 509. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
7pgt
Structure name
the structure of human neurofibromin isoform 2 in opened conformation
Structure deposition date
2021-08-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
17
Peptide accession
P21359
Residue number A
434
Residue number B
509
Peptide name
Neurofibromin
Ligandability
Cysteine 434 of Neurofibromin
Cysteine 509 of Neurofibromin
7pgu F 328 F 379
A redox-regulated disulphide may form within Neurofibromin between cysteines 328 and 379. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
7pgu
Structure name
autoinhibited structure of human neurofibromin isoform 2 stabilized by zinc
Structure deposition date
2021-08-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
17
% buried
96
Peptide accession
P21359
Residue number A
328
Residue number B
379
Peptide name
Neurofibromin
Ligandability
Cysteine 328 of Neurofibromin
Cysteine 379 of Neurofibromin
7pgs N 245 N 277
A redox-regulated disulphide may form within Neurofibromin between cysteines 245 and 277. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
7pgs
Structure name
consensus structure of human neurofibromin isoform 2
Structure deposition date
2021-08-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
68
Peptide accession
P21359
Residue number A
245
Residue number B
277
Peptide name
Neurofibromin
Ligandability
Cysteine 245 of Neurofibromin
Cysteine 277 of Neurofibromin
7pgu F 582 F 709
A redox-regulated disulphide may form within Neurofibromin between cysteines 582 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
7pgu
Structure name
autoinhibited structure of human neurofibromin isoform 2 stabilized by zinc
Structure deposition date
2021-08-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
90
Peptide accession
P21359
Residue number A
582
Residue number B
709
Peptide name
Neurofibromin
Ligandability
Cysteine 582 of Neurofibromin
Cysteine 709 of Neurofibromin
7r03 B 709 B 714
A redox-regulated disulphide may form within Neurofibromin between cysteines 709 and 714. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
7r03
Structure name
neurofibromin occluded conformation
Structure deposition date
2022-02-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
80
Peptide accession
P21359
Residue number A
709
Residue number B
714
Peptide name
Neurofibromin
Ligandability
Cysteine 709 of Neurofibromin
Cysteine 714 of Neurofibromin
7pgt F 379 F 397
A redox-regulated disulphide may form within Neurofibromin between cysteines 379 and 397. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
7pgt
Structure name
the structure of human neurofibromin isoform 2 in opened conformation
Structure deposition date
2021-08-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
90
Peptide accession
P21359
Residue number A
379
Residue number B
397
Peptide name
Neurofibromin
Ligandability
Cysteine 379 of Neurofibromin
Cysteine 397 of Neurofibromin
6v6f B 1288 B 1367
A redox-regulated disulphide may form within Neurofibromin between cysteines 1288 and 1367. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6v6f
Structure name
crystal structure of q61l kras(gmppnp)-nf1(grd)-spred1(evh1) complex
Structure deposition date
2019-12-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
100
Peptide accession
P21359
Residue number A
1288
Residue number B
1367
Peptide name
Neurofibromin
Ligandability
Cysteine 1288 of Neurofibromin
Cysteine 1367 of Neurofibromin
6v65 B 1288 B 1365
A redox-regulated disulphide may form within Neurofibromin between cysteines 1288 and 1365. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
6v65
Structure name
crystal structure of kras(gmppnp)-nf1(grd)-spred1 complex
Structure deposition date
2019-12-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
P21359
Residue number A
1288
Residue number B
1365
Peptide name
Neurofibromin
Ligandability
Cysteine 1288 of Neurofibromin
Cysteine 1365 of Neurofibromin
6v6f B 1365 B 1367
A redox-regulated disulphide may form within Neurofibromin between cysteines 1365 and 1367. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
6v6f
Structure name
crystal structure of q61l kras(gmppnp)-nf1(grd)-spred1(evh1) complex
Structure deposition date
2019-12-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
P21359
Residue number A
1365
Residue number B
1367
Peptide name
Neurofibromin
Ligandability
Cysteine 1365 of Neurofibromin
Cysteine 1367 of Neurofibromin
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