Androgen receptor

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Androgen receptor

Peptide B name

Androgen receptor

Peptide A accession

Peptide B accession

Peptide A residue number

584

Peptide B residue number

584

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 578 and 584.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

578

Residue number B

584

Peptide name

Androgen receptor

Ligandability

Cysteine 578 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 584 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 559 and 562.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

559

Residue number B

562

Peptide name

Androgen receptor

Ligandability

Cysteine 559 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 562 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 542 and 562.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide accession

Residue number A

542

Residue number B

562

Peptide name

Androgen receptor

Ligandability

Cysteine 542 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 562 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 578 and 597.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

578

Residue number B

597

Peptide name

Androgen receptor

Ligandability

Cysteine 578 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 597 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 594 and 597.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

594

Residue number B

597

Peptide name

Androgen receptor

Ligandability

Cysteine 594 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 597 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 545 and 562.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

545

Residue number B

562

Peptide name

Androgen receptor

Ligandability

Cysteine 545 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 562 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 578 and 594.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

578

Residue number B

594

Peptide name

Androgen receptor

Ligandability

Cysteine 578 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 594 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 584 and 597.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

584

Residue number B

597

Peptide name

Androgen receptor

Ligandability

Cysteine 584 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 597 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 584 and 594.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

584

Residue number B

594

Peptide name

Androgen receptor

Ligandability

Cysteine 584 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 594 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 542 and 545.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide accession

Residue number A

542

Residue number B

545

Peptide name

Androgen receptor

Ligandability

Cysteine 542 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 545 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 545 and 559.

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

545

Residue number B

559

Peptide name

Androgen receptor

Ligandability

Cysteine 545 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 559 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 670 and 845 (669 and 844 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

1t63

Structure name

crystal structure of the androgen receptor ligand binding domain with dht and a peptide derived from its physiological coactivator grip1 nr box3

Structure deposition date

2004-05-05

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

% buried

nan

Peptide accession

P10275

Residue number A

670

Residue number B

845

Peptide name

Androgen receptor

Ligandability

Cysteine 670 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 845 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 562 and 602. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

562

Residue number B

602

Peptide name

Androgen receptor

Ligandability

Cysteine 562 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 602 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 670 and 853 (669 and 852 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

5jjm

Structure name

crystal structure of homodimeric androgen receptor ligand-binding domain bound to dht and lxxll peptide

Structure deposition date

2016-04-24

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

% buried

nan

Peptide accession

P10275

Residue number A

670

Residue number B

853

Peptide name

Androgen receptor

Ligandability

Cysteine 670 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 853 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 845 and 853 (844 and 852 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

1xj7

Structure name

complex androgen receptor lbd and rac3 peptide

Structure deposition date

2004-09-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P10275

Residue number A

845

Residue number B

853

Peptide name

Androgen receptor

Ligandability

Cysteine 845 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 853 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 542 and 602. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide accession

Residue number A

542

Residue number B

602

Peptide name

Androgen receptor

Ligandability

Cysteine 542 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 602 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 542 and 559. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

nan

Peptide accession

Residue number A

542

Residue number B

559

Peptide name

Androgen receptor

Ligandability

Cysteine 542 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 559 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 789 and 827 (806 and 844 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

1i38

Structure name

crystal structure of the rat androgen receptor ligand binding domain t877a mutant complex with dihydrotestosterone

Structure deposition date

2001-02-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

789

Residue number B

827

Peptide name

Androgen receptor

Ligandability

Cysteine 789 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 827 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Androgen receptor between cysteines 559 and 602. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of androgen receptor dna-binding domain bound to a direct repeat response element

Structure deposition date

2003-10-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Residue number A

559

Residue number B

602

Peptide name

Androgen receptor

Ligandability

Cysteine 559 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.

Cysteine 602 of Androgen receptor

Not ligandable in the dataset of Vinogradova et al.