Rhodopsin
Intermolecular
Cysteine 140 and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 140 and cysteine 351 of Guanine nucleotide-binding protein G(o) subunit alpha
Cysteine 140 and cysteine 351 of Guanine nucleotide-binding protein G(t) subunit alpha-3
Cysteine 140 and cysteine 347 of Guanine nucleotide-binding protein G(t) subunit alpha-1
Intramolecular
Cysteine 322 and cysteine 323
Cysteine 110 and cysteine 187
Cysteine 110 and cysteine 185
Cysteine 140 and cysteine 222
Cysteine 316 and cysteine 322
Cysteine 185 and cysteine 187
More...Cysteine 316 and cysteine 323
Cysteine 110 and cysteine 282
Cysteine 187 and cysteine 282
6cmo R 140 A 351
A redox-regulated disulphide may form between cysteine 140 of Rhodopsin and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6cmo
Structure name
rhodopsin-gi complex
Structure deposition date
2018-03-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
64
Peptide A name
Rhodopsin
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P08100
Peptide B accession
P63096
Peptide A residue number
140
Peptide B residue number
351
Ligandability
Cysteine 140 of Rhodopsin
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
6fuf A 140 B 351
A redox-regulated disulphide may form between cysteine 140 of Rhodopsin and cysteine 351 of Guanine nucleotide-binding protein G(o) subunit alpha. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6fuf
Structure name
crystal structure of the rhodopsin-mini-go complex
Structure deposition date
2018-02-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
76
Peptide A name
Rhodopsin
Peptide B name
Guanine nucleotide-binding protein G(o) subunit alpha
Peptide A accession
P02699
Peptide B accession
P09471
Peptide A residue number
140
Peptide B residue number
351
Ligandability
Cysteine 140 of Rhodopsin
Cysteine 351 of Guanine nucleotide-binding protein G(o) subunit alpha
4a4m A 140 B 347
A redox-regulated disulphide may form between cysteine 140 of Rhodopsin and cysteine 351 of Guanine nucleotide-binding protein G(t) subunit alpha-3 (140 and 347 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
4a4m
Structure name
crystal structure of the light-activated constitutively active n2c, m257y,d282c rhodopsin mutant in complex with a peptide resembling the c-terminus of the galpha-protein subunit (gact)
Structure deposition date
2011-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
74
Peptide A name
Rhodopsin
Peptide B name
Guanine nucleotide-binding protein G(t) subunit alpha-3
Peptide A accession
P02699
Peptide B accession
P0C7Q4
Peptide A residue number
140
Peptide B residue number
351
Ligandability
Cysteine 140 of Rhodopsin
Cysteine 351 of Guanine nucleotide-binding protein G(t) subunit alpha-3
3dqb A 140 B 347
A redox-regulated disulphide may form between cysteine 140 of Rhodopsin and cysteine 347 of Guanine nucleotide-binding protein G(t) subunit alpha-1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
3dqb
Structure name
crystal structure of the active g-protein-coupled receptor opsin in complex with a c-terminal peptide derived from the galpha subunit of transducin
Structure deposition date
2008-07-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
79
Peptide A name
Rhodopsin
Peptide B name
Guanine nucleotide-binding protein G(t) subunit alpha-1
Peptide A accession
P02699
Peptide B accession
P04695
Peptide A residue number
140
Peptide B residue number
347
Ligandability
Cysteine 140 of Rhodopsin
Cysteine 347 of Guanine nucleotide-binding protein G(t) subunit alpha-1
2i37 A 322 A 323
A redox-regulated disulphide may form within Rhodopsin between cysteines 322 and 323.
Details
Redox score ?
81
PDB code
2i37
Structure name
crystal structure of a photoactivated rhodopsin
Structure deposition date
2006-08-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
32
Minimum pKa ?
8
% buried
0
Peptide accession
P02699
Residue number A
322
Residue number B
323
Peptide name
Rhodopsin
Ligandability
Cysteine 322 of Rhodopsin
Cysteine 323 of Rhodopsin
3oax A 110 A 187
A redox-regulated disulphide may form within Rhodopsin between cysteines 110 and 187.
Details
Redox score ?
80
PDB code
3oax
Structure name
crystal structure of bovine rhodopsin with beta-ionone
Structure deposition date
2010-08-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02699
Residue number A
110
Residue number B
187
Peptide name
Rhodopsin
Ligandability
Cysteine 110 of Rhodopsin
Cysteine 187 of Rhodopsin
1jfp A 110 A 185
A redox-regulated disulphide may form within Rhodopsin between cysteines 110 and 185. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1jfp
Structure name
structure of bovine rhodopsin (dark adapted)
Structure deposition date
2001-06-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
nan
Peptide accession
P02699
Residue number A
110
Residue number B
185
Peptide name
Rhodopsin
Ligandability
Cysteine 110 of Rhodopsin
Cysteine 185 of Rhodopsin
6cmo R 140 R 222
A redox-regulated disulphide may form within Rhodopsin between cysteines 140 and 222. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6cmo
Structure name
rhodopsin-gi complex
Structure deposition date
2018-03-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
48
Peptide accession
P08100
Residue number A
140
Residue number B
222
Peptide name
Rhodopsin
Ligandability
Cysteine 140 of Rhodopsin
Cysteine 222 of Rhodopsin
1jfp A 316 A 322
A redox-regulated disulphide may form within Rhodopsin between cysteines 316 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
1jfp
Structure name
structure of bovine rhodopsin (dark adapted)
Structure deposition date
2001-06-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
34
Peptide accession
P02699
Residue number A
316
Residue number B
322
Peptide name
Rhodopsin
Ligandability
Cysteine 316 of Rhodopsin
Cysteine 322 of Rhodopsin
6cmo R 185 R 187
A redox-regulated disulphide may form within Rhodopsin between cysteines 185 and 187. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6cmo
Structure name
rhodopsin-gi complex
Structure deposition date
2018-03-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
nan
Peptide accession
P08100
Residue number A
185
Residue number B
187
Peptide name
Rhodopsin
Ligandability
Cysteine 185 of Rhodopsin
Cysteine 187 of Rhodopsin
1jfp A 316 A 323
A redox-regulated disulphide may form within Rhodopsin between cysteines 316 and 323. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
1jfp
Structure name
structure of bovine rhodopsin (dark adapted)
Structure deposition date
2001-06-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
44
Peptide accession
P02699
Residue number A
316
Residue number B
323
Peptide name
Rhodopsin
Ligandability
Cysteine 316 of Rhodopsin
Cysteine 323 of Rhodopsin
6qno R 2 R 282
A redox-regulated disulphide may form within Rhodopsin between cysteines 110 and 282 (2 and 282 respectively in this structure).
Details
Redox score ?
nan
PDB code
6qno
Structure name
rhodopsin-gi protein complex
Structure deposition date
2019-02-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02699
Residue number A
110
Residue number B
282
Peptide name
Rhodopsin
Ligandability
Cysteine 110 of Rhodopsin
Cysteine 282 of Rhodopsin
Uncertain whether structure cysteine 2 has been assigned to correct residue.
Cysteine 282 in protein B could not be asigned to a Uniprot residue.
6cmo R 2 R 282
A redox-regulated disulphide may form within Rhodopsin between cysteines 187 and 282 (2 and 282 respectively in this structure).
Details
Redox score ?
nan
PDB code
6cmo
Structure name
rhodopsin-gi complex
Structure deposition date
2018-03-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08100
Residue number A
187
Residue number B
282
Peptide name
Rhodopsin
Ligandability
Cysteine 187 of Rhodopsin
Cysteine 282 of Rhodopsin
Uncertain whether structure cysteine 2 has been assigned to correct residue.
Cysteine 282 in protein B could not be asigned to a Uniprot residue.
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