ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Retinoblastoma-associated protein

Intermolecular
Cysteine 438 and cysteine 438
Cysteine 105 of Large T antigen and cysteine 706
Intramolecular
Cysteine 278 and cysteine 283
Cysteine 666 and cysteine 712
Cysteine 221 and cysteine 278
Cysteine 489 and cysteine 553
Cysteine 61 and cysteine 102
Cysteine 221 and cysteine 283
A redox-regulated disulphide may form between two units of Retinoblastoma-associated protein at cysteines 438 and 438.

Details

Redox score ?
81
PDB code
1o9k
Structure name
crystal structure of the retinoblastoma tumour suppressor protein bound to e2f peptide
Structure deposition date
2002-12-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
44
Peptide A name
Retinoblastoma-associated protein
Peptide B name
Retinoblastoma-associated protein
Peptide A accession
P06400
Peptide B accession
P06400
Peptide A residue number
438
Peptide B residue number
438

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 between cysteine 105 of Large T antigen and cysteine 706 of Retinoblastoma-associated protein. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1gh6
Structure name
retinoblastoma pocket complexed with sv40 large t antigen
Structure deposition date
2000-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
78
Peptide A name
Large T antigen
Peptide B name
Retinoblastoma-associated protein
Peptide A accession
P03070
Peptide B accession
P06400
Peptide A residue number
105
Peptide B residue number
706

Ligandability

Cysteine 105 of Large T antigen

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 706 of Retinoblastoma-associated protein

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 Retinoblastoma-associated protein between cysteines 278 and 283.

Details

Redox score ?
68
PDB code
2qdj
Structure name
crystal structure of the retinoblastoma protein n-domain provides insight into tumor suppression, ligand interaction and holoprotein architecture
Structure deposition date
2007-06-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
49
Minimum pKa ?
10
% buried
34
Peptide accession
P06400
Residue number A
278
Residue number B
283
Peptide name
Retinoblastoma-associated protein

Ligandability

Cysteine 278 of Retinoblastoma-associated protein

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 283 of Retinoblastoma-associated protein

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 Retinoblastoma-associated protein between cysteines 666 and 712. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
1o9k
Structure name
crystal structure of the retinoblastoma tumour suppressor protein bound to e2f peptide
Structure deposition date
2002-12-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
72
Peptide accession
P06400
Residue number A
666
Residue number B
712
Peptide name
Retinoblastoma-associated protein

Ligandability

Cysteine 666 of Retinoblastoma-associated protein

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 712 of Retinoblastoma-associated protein

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 Retinoblastoma-associated protein between cysteines 221 and 278. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2qdj
Structure name
crystal structure of the retinoblastoma protein n-domain provides insight into tumor suppression, ligand interaction and holoprotein architecture
Structure deposition date
2007-06-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
58
Peptide accession
P06400
Residue number A
221
Residue number B
278
Peptide name
Retinoblastoma-associated protein

Ligandability

Cysteine 221 of Retinoblastoma-associated protein

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 278 of Retinoblastoma-associated protein

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 Retinoblastoma-associated protein between cysteines 489 and 553. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2r7g
Structure name
structure of the retinoblastoma protein pocket domain in complex with adenovirus e1a cr1 domain
Structure deposition date
2007-09-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
90
Peptide accession
P06400
Residue number A
489
Residue number B
553
Peptide name
Retinoblastoma-associated protein

Ligandability

Cysteine 489 of Retinoblastoma-associated protein

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 553 of Retinoblastoma-associated protein

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 Retinoblastoma-associated protein between cysteines 61 and 102. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
4elj
Structure name
crystal structure of the inactive retinoblastoma protein phosphorylated at t373
Structure deposition date
2012-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
74
Peptide accession
P06400
Residue number A
61
Residue number B
102
Peptide name
Retinoblastoma-associated protein

Ligandability

Cysteine 61 of Retinoblastoma-associated protein

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 102 of Retinoblastoma-associated protein

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 Retinoblastoma-associated protein between cysteines 221 and 283. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
4elj
Structure name
crystal structure of the inactive retinoblastoma protein phosphorylated at t373
Structure deposition date
2012-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
91
Peptide accession
P06400
Residue number A
221
Residue number B
283
Peptide name
Retinoblastoma-associated protein

Ligandability

Cysteine 221 of Retinoblastoma-associated protein

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 283 of Retinoblastoma-associated protein

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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