ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein farnesyltransferase subunit beta

Intermolecular
Cysteine 299 and cysteine 186 of GTPase KRas
Cysteine 95 and cysteine 186 of GTPase KRas
Cysteine 366 and cysteine 186 of GTPase KRas
Intramolecular
Cysteine 343 and cysteine 366
Cysteine 342 and cysteine 343
Cysteine 206 and cysteine 254
Cysteine 299 and cysteine 366
Cysteine 104 and cysteine 133
Cysteine 299 and cysteine 343
Cysteine 104 and cysteine 127
More...
Cysteine 364 and cysteine 366
Cysteine 342 and cysteine 366
Cysteine 299 and cysteine 364
A redox-regulated disulphide may form between cysteine 299 of Protein farnesyltransferase subunit beta and cysteine 186 of GTPase KRas (299 and 8 respectively in this structure).

Details

Redox score ?
76
PDB code
1d8d
Structure name
co-crystal structure of rat protein farnesyltransferase complexed with a k-ras4b peptide substrate and fpp analog at 2
Structure deposition date
1999-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
5
% buried
100
Peptide A name
Protein farnesyltransferase subunit beta
Peptide B name
GTPase KRas
Peptide A accession
Q02293
Peptide B accession
P01116
Peptide A residue number
299
Peptide B residue number
186

Ligandability

Cysteine 299 of Protein farnesyltransferase subunit beta

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 186 of GTPase KRas

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 between cysteine 95 of Protein farnesyltransferase subunit beta and cysteine 186 of GTPase KRas (95 and 8 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1kzo
Structure name
protein farnesyltransferase complexed with farnesylated k-ras4b peptide product and farnesyl diphosphate substrate bound simultaneously
Structure deposition date
2002-02-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
12
% buried
94
Peptide A name
Protein farnesyltransferase subunit beta
Peptide B name
GTPase KRas
Peptide A accession
Q02293
Peptide B accession
P01118
Peptide A residue number
95
Peptide B residue number
186

Ligandability

Cysteine 95 of Protein farnesyltransferase subunit beta

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 186 of GTPase KRas

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 between cysteine 366 of Protein farnesyltransferase subunit beta and cysteine 186 of GTPase KRas (366 and 8 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1d8d
Structure name
co-crystal structure of rat protein farnesyltransferase complexed with a k-ras4b peptide substrate and fpp analog at 2
Structure deposition date
1999-10-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
5
% buried
100
Peptide A name
Protein farnesyltransferase subunit beta
Peptide B name
GTPase KRas
Peptide A accession
Q02293
Peptide B accession
P01116
Peptide A residue number
366
Peptide B residue number
186

Ligandability

Cysteine 366 of Protein farnesyltransferase subunit beta

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 186 of GTPase KRas

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 Protein farnesyltransferase subunit beta between cysteines 343 and 366.

Details

Redox score ?
61
PDB code
1jcq
Structure name
crystal structure of human protein farnesyltransferase complexed with farnesyl diphosphate and the peptidomimetic inhibitor l-739,750
Structure deposition date
2001-06-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
98
Minimum pKa ?
10
% buried
100
Peptide accession
P49356
Residue number A
343
Residue number B
366
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 343 of Protein farnesyltransferase subunit beta

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 366 of Protein farnesyltransferase subunit beta

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 Protein farnesyltransferase subunit beta between cysteines 342 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
1jcr
Structure name
crystal structure of rat protein farnesyltransferase complexed with the non-substrate tetrapeptide inhibitor cvfm and farnesyl diphosphate substrate
Structure deposition date
2001-06-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
90
Minimum pKa ?
10
% buried
100
Peptide accession
Q02293
Residue number A
342
Residue number B
343
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 342 of Protein farnesyltransferase subunit beta

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 343 of Protein farnesyltransferase subunit beta

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 Protein farnesyltransferase subunit beta between cysteines 206 and 254. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2f0y
Structure name
crystal structure of human protein farnesyltransferase complexed with farnesyl diphosphate and hydantoin derivative
Structure deposition date
2005-11-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
P49356
Residue number A
206
Residue number B
254
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 206 of Protein farnesyltransferase subunit beta

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 254 of Protein farnesyltransferase subunit beta

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 Protein farnesyltransferase subunit beta between cysteines 299 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1x81
Structure name
farnesyl transferase structure of jansen compound
Structure deposition date
2004-08-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide accession
Q02293
Residue number A
299
Residue number B
366
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 299 of Protein farnesyltransferase subunit beta

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 366 of Protein farnesyltransferase subunit beta

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 Protein farnesyltransferase subunit beta between cysteines 104 and 133 (604 and 633 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2h6i
Structure name
w102t/y365f protein farnesyltransferase double mutant complexed with a geranylgeranylated ddptasacvls peptide product at 3
Structure deposition date
2006-05-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
P49356
Residue number A
104
Residue number B
133
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 104 of Protein farnesyltransferase subunit beta

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 133 of Protein farnesyltransferase subunit beta

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 Protein farnesyltransferase subunit beta between cysteines 299 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1x81
Structure name
farnesyl transferase structure of jansen compound
Structure deposition date
2004-08-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
10
% buried
100
Peptide accession
Q02293
Residue number A
299
Residue number B
343
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 299 of Protein farnesyltransferase subunit beta

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 343 of Protein farnesyltransferase subunit beta

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 Protein farnesyltransferase subunit beta between cysteines 104 and 127. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
1n95
Structure name
aryl tetrahydrophyridine inhbitors of farnesyltranferase: glycine, phenylalanine and histidine derivatives
Structure deposition date
2002-11-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
79
Peptide accession
Q02293
Residue number A
104
Residue number B
127
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 104 of Protein farnesyltransferase subunit beta

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 127 of Protein farnesyltransferase subunit beta

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 Protein farnesyltransferase subunit beta between cysteines 364 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
1x81
Structure name
farnesyl transferase structure of jansen compound
Structure deposition date
2004-08-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
13
% buried
100
Peptide accession
Q02293
Residue number A
364
Residue number B
366
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 364 of Protein farnesyltransferase subunit beta

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 366 of Protein farnesyltransferase subunit beta

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 Protein farnesyltransferase subunit beta between cysteines 342 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
1ni1
Structure name
imidazole and cyanophenyl farnesyl transferase inhibitors
Structure deposition date
2002-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
Q02293
Residue number A
342
Residue number B
366
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 342 of Protein farnesyltransferase subunit beta

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 366 of Protein farnesyltransferase subunit beta

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 Protein farnesyltransferase subunit beta between cysteines 299 and 364. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
20
PDB code
1ni1
Structure name
imidazole and cyanophenyl farnesyl transferase inhibitors
Structure deposition date
2002-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
Q02293
Residue number A
299
Residue number B
364
Peptide name
Protein farnesyltransferase subunit beta

Ligandability

Cysteine 299 of Protein farnesyltransferase subunit beta

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 364 of Protein farnesyltransferase subunit beta

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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