Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Cellular tumor antigen p53 at cysteines 238 and 182. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1tup

Structure name

tumor suppressor p53 complexed with dna

Structure deposition date

1995-07-11

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Cellular tumor antigen p53

Peptide B name

Cellular tumor antigen p53

Peptide A accession

Peptide B accession

Peptide A residue number

238

Peptide B residue number

182

Ligandability

Cysteine 238 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 182 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 176 and 242.

Details

Redox score ?

PDB code

6sl6

Structure name

p53 charged core

Structure deposition date

2019-08-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

176

Residue number B

242

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 176 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 242 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 238 and 242.

Details

Redox score ?

PDB code

Structure name

the structure of the oncoprotein sv40 large t antigen and p53 tumor suppressor complex

Structure deposition date

2006-05-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide accession

Residue number A

238

Residue number B

242

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 238 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 242 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 124 and 135.

Details

Redox score ?

PDB code

7v97

Structure name

arsenic-bound p53 dna-binding domain mutant v272m

Structure deposition date

2021-08-24

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

124

Residue number B

135

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 124 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 135 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 176 and 238.

Details

Redox score ?

PDB code

5ecg

Structure name

crystal structure of the brct domains of 53bp1 in complex with p53 and h2ax-pser139 (gammah2ax)

Structure deposition date

2015-10-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

176

Residue number B

238

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 176 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 238 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 135 and 141.

Details

Redox score ?

PDB code

Structure name

the structure of the oncoprotein sv40 large t antigen and p53 tumor suppressor complex

Structure deposition date

2006-05-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

135

Residue number B

141

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 135 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 141 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 124 and 141.

Details

Redox score ?

PDB code

Structure name

the structure of the oncoprotein sv40 large t antigen and p53 tumor suppressor complex

Structure deposition date

2006-05-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

124

Residue number B

141

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 124 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 141 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 275 and 277. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

the structure of the oncoprotein sv40 large t antigen and p53 tumor suppressor complex

Structure deposition date

2006-05-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

275

Residue number B

277

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 275 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 277 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 176 and 182. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

the structure of the oncoprotein sv40 large t antigen and p53 tumor suppressor complex

Structure deposition date

2006-05-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

176

Residue number B

182

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 176 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 182 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 182 and 242. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4ibz

Structure name

human p53 core domain with hot spot mutation r273c and second-site suppressor mutation t284r

Structure deposition date

2012-12-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

182

Residue number B

242

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 182 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 242 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 135 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

the structure of the oncoprotein sv40 large t antigen and p53 tumor suppressor complex

Structure deposition date

2006-05-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

Residue number A

135

Residue number B

275

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 135 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 275 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 182 and 238. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

the structure of the oncoprotein sv40 large t antigen and p53 tumor suppressor complex

Structure deposition date

2006-05-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

182

Residue number B

238

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 182 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 238 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 242 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2fej

Structure name

solution structure of human p53 dna binding domain

Structure deposition date

2005-12-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

242

Residue number B

275

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 242 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 275 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 135 and 277. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2fej

Structure name

solution structure of human p53 dna binding domain

Structure deposition date

2005-12-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

135

Residue number B

277

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 135 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 277 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 135 and 1844 (1828 and 1844 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5hp0

Structure name

solution structure of taz2-p53ad2

Structure deposition date

2016-01-19

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

135

Residue number B

1844

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 135 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1844 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1844 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 141 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

the structure of the oncoprotein sv40 large t antigen and p53 tumor suppressor complex

Structure deposition date

2006-05-16

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

141

Residue number B

275

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 141 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 275 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 124 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4loe

Structure name

human p53 core domain mutant n239y

Structure deposition date

2013-07-12

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

124

Residue number B

275

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 124 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 275 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 275 and 275 (273 and 275 respectively in this structure).

Details

Redox score ?

nan

PDB code

4ibq

Structure name

human p53 core domain with hot spot mutation r273c

Structure deposition date

2012-12-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

275

Residue number B

275

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 275 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 275 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Uncertain whether structure cysteine 273 has been assigned to correct residue.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 141 and 141 (1784 and 1827 respectively in this structure).

Details

Redox score ?

nan

PDB code

5hpd

Structure name

solution structure of taz2-p53tad

Structure deposition date

2016-01-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

141

Residue number B

141

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 141 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 141 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Uncertain whether structure cysteine 1784 has been assigned to correct residue.

Uncertain whether structure cysteine 1827 has been assigned to correct residue.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 141 and 182 (1827 and 1834 respectively in this structure).

Details

Redox score ?

nan

PDB code

5hp0

Structure name

solution structure of taz2-p53ad2

Structure deposition date

2016-01-19

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

141

Residue number B

182

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 141 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 182 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Uncertain whether structure cysteine 1827 has been assigned to correct residue.

Uncertain whether structure cysteine 1834 has been assigned to correct residue.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 141 and 277 (1784 and 1786 respectively in this structure).

Details

Redox score ?

nan

PDB code

5hp0

Structure name

solution structure of taz2-p53ad2

Structure deposition date

2016-01-19

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

141

Residue number B

277

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 141 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 277 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Uncertain whether structure cysteine 1784 has been assigned to correct residue.

Uncertain whether structure cysteine 1786 has been assigned to correct residue.

A redox-regulated disulphide may form within Cellular tumor antigen p53 between cysteines 277 and 1791 (1786 and 1791 respectively in this structure).

Details

Redox score ?

nan

PDB code

5hpd

Structure name

solution structure of taz2-p53tad

Structure deposition date

2016-01-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

277

Residue number B

1791

Peptide name

Cellular tumor antigen p53

Ligandability

Cysteine 277 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1791 of Cellular tumor antigen p53

Not ligandable in the dataset of Vinogradova et al.