ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Adenylate cyclase type 5

Intramolecular
Cysteine 513 and cysteine 525
Cysteine 513 and cysteine 540
Cysteine 513 and cysteine 539
Cysteine 525 and cysteine 540
Cysteine 539 and cysteine 540
Cysteine 525 and cysteine 539
A redox-regulated disulphide may form within Adenylate cyclase type 5 between cysteines 513 and 525 (432 and 444 respectively in this structure).

Details

Redox score ?
75
PDB code
1cjv
Structure name
complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with beta-l-2',3'-dideoxyatp, mg, and zn
Structure deposition date
1999-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
4
% buried
96
Peptide accession
P30803
Residue number A
513
Residue number B
525
Peptide name
Adenylate cyclase type 5

Ligandability

Cysteine 513 of Adenylate cyclase type 5

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 525 of Adenylate cyclase type 5

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 Adenylate cyclase type 5 between cysteines 513 and 540 (432 and 459 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
3c14
Structure name
complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with pyrophosphate and ca
Structure deposition date
2008-01-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
14
% buried
95
Peptide accession
P30803
Residue number A
513
Residue number B
540
Peptide name
Adenylate cyclase type 5

Ligandability

Cysteine 513 of Adenylate cyclase type 5

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 540 of Adenylate cyclase type 5

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 Adenylate cyclase type 5 between cysteines 513 and 539 (432 and 458 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
1tl7
Structure name
complex of gs- with the catalytic domains of mammalian adenylyl cyclase: complex with 2'(3')-o-(n- methylanthraniloyl)-guanosine 5'-triphosphate and mn
Structure deposition date
2004-06-09
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
69
Peptide accession
P30803
Residue number A
513
Residue number B
539
Peptide name
Adenylate cyclase type 5

Ligandability

Cysteine 513 of Adenylate cyclase type 5

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 539 of Adenylate cyclase type 5

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 Adenylate cyclase type 5 between cysteines 525 and 540 (444 and 459 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
3c14
Structure name
complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with pyrophosphate and ca
Structure deposition date
2008-01-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
90
Minimum pKa ?
10
% buried
100
Peptide accession
P30803
Residue number A
525
Residue number B
540
Peptide name
Adenylate cyclase type 5

Ligandability

Cysteine 525 of Adenylate cyclase type 5

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 540 of Adenylate cyclase type 5

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 Adenylate cyclase type 5 between cysteines 539 and 540 (458 and 459 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1cjk
Structure name
complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with adenosine 5'-(alpha thio)-triphosphate (rp), mg, and mn
Structure deposition date
1999-04-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
69
Peptide accession
P30803
Residue number A
539
Residue number B
540
Peptide name
Adenylate cyclase type 5

Ligandability

Cysteine 539 of Adenylate cyclase type 5

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 540 of Adenylate cyclase type 5

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 Adenylate cyclase type 5 between cysteines 525 and 539 (444 and 458 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2gvd
Structure name
complex of gs- with the catalytic domains of mammalian adenylyl cyclase: complex with tnp-atp and mn
Structure deposition date
2006-05-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
10
% buried
nan
Peptide accession
P30803
Residue number A
525
Residue number B
539
Peptide name
Adenylate cyclase type 5

Ligandability

Cysteine 525 of Adenylate cyclase type 5

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 539 of Adenylate cyclase type 5

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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