Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Intermolecular
Cysteine 911 of Adenylate cyclase type 2 and cysteine 237
Intramolecular
Cysteine 174 and cysteine 162
Cysteine 174 and cysteine 200
Cysteine 200 and cysteine 162
Cysteine 3 and cysteine 452
Cysteine 200 and cysteine 563
Cysteine 449 and cysteine 452
2gvz B 911 C 237
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
6au6 A 174 A 201
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(s) subunit alpha isoforms short between cysteines 174 and 162 (174 and 201 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6au6
Structure name
crystal structure of gdp-bound human gnas r201c mutant
Structure deposition date
2017-08-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
69
Minimum pKa ?
13
% buried
100
Peptide accession
P63092
Residue number A
174
Residue number B
162
Peptide name
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Ligandability
Cysteine 174 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Cysteine 162 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Uncertain whether structure cysteine 201 has been assigned to correct residue.
6au6 A 174 A 200
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(s) subunit alpha isoforms short between cysteines 174 and 200. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
6au6
Structure name
crystal structure of gdp-bound human gnas r201c mutant
Structure deposition date
2017-08-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
95
Peptide accession
P63092
Residue number A
174
Residue number B
200
Peptide name
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Ligandability
Cysteine 174 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Cysteine 200 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
6au6 A 200 A 201
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(s) subunit alpha isoforms short between cysteines 200 and 162 (200 and 201 respectively in this structure).
Details
Redox score ?
nan
PDB code
6au6
Structure name
crystal structure of gdp-bound human gnas r201c mutant
Structure deposition date
2017-08-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
95
Peptide accession
P63092
Residue number A
200
Residue number B
162
Peptide name
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Ligandability
Cysteine 200 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Cysteine 162 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Uncertain whether structure cysteine 201 has been assigned to correct residue.
7tmw R 420 R 452
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(s) subunit alpha isoforms short between cysteines 3 and 452 (420 and 452 respectively in this structure).
Details
Redox score ?
nan
PDB code
7tmw
Structure name
cryo-em structure of the relaxin receptor rxfp1 in complex with heterotrimeric gs
Structure deposition date
2022-01-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
40
Peptide accession
P63092
Residue number A
3
Residue number B
452
Peptide name
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Ligandability
Cysteine 3 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Cysteine 452 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Uncertain whether structure cysteine 420 has been assigned to correct residue.
Cysteine 452 in protein B could not be asigned to a Uniprot residue.
7tmw R 485 R 563
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(s) subunit alpha isoforms short between cysteines 200 and 563 (485 and 563 respectively in this structure).
Details
Redox score ?
nan
PDB code
7tmw
Structure name
cryo-em structure of the relaxin receptor rxfp1 in complex with heterotrimeric gs
Structure deposition date
2022-01-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P63092
Residue number A
200
Residue number B
563
Peptide name
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Ligandability
Cysteine 200 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Cysteine 563 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Uncertain whether structure cysteine 485 has been assigned to correct residue.
Cysteine 563 in protein B could not be asigned to a Uniprot residue.
7tmw R 449 R 452
A redox-regulated disulphide may form within Guanine nucleotide-binding protein G(s) subunit alpha isoforms short between cysteines 449 and 452.
Details
Redox score ?
nan
PDB code
7tmw
Structure name
cryo-em structure of the relaxin receptor rxfp1 in complex with heterotrimeric gs
Structure deposition date
2022-01-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
50
Peptide accession
P63092
Residue number A
449
Residue number B
452
Peptide name
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Ligandability
Cysteine 449 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Cysteine 452 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Cysteine 449 in protein A could not be asigned to a Uniprot residue.
Cysteine 452 in protein B could not be asigned to a Uniprot residue.
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