ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Adenylate cyclase type 2

Intermolecular
Cysteine 911 and cysteine 237 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Intramolecular
Cysteine 1056 and cysteine 1058
Cysteine 884 and cysteine 886
A redox-regulated disulphide may form between cysteine 911 of Adenylate cyclase type 2 and cysteine 237 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2gvz
Structure name
crystal structure of complex of gs- with the catalytic domains of mammalian adenylyl cyclase: complex with mant-atp and mn
Structure deposition date
2006-05-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
100
Peptide A name
Adenylate cyclase type 2
Peptide B name
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Peptide A accession
P26769
Peptide B accession
P04896
Peptide A residue number
911
Peptide B residue number
237

Ligandability

Cysteine 911 of Adenylate cyclase type 2

Cysteine 237 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short

A redox-regulated disulphide may form within Adenylate cyclase type 2 between cysteines 1056 and 1058. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
1cs4
Structure name
complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with 2'-deoxy-adenosine 3'-monophosphate, pyrophosphate and mg
Structure deposition date
1999-08-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
20
Peptide accession
P26769
Residue number A
1056
Residue number B
1058
Peptide name
Adenylate cyclase type 2

Ligandability

Cysteine 1056 of Adenylate cyclase type 2

Cysteine 1058 of Adenylate cyclase type 2

A redox-regulated disulphide may form within Adenylate cyclase type 2 between cysteines 884 and 886. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
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)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
62
Peptide accession
P26769
Residue number A
884
Residue number B
886
Peptide name
Adenylate cyclase type 2

Ligandability

Cysteine 884 of Adenylate cyclase type 2

Cysteine 886 of Adenylate cyclase type 2

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