Oxytocin receptor
Intramolecular
Cysteine 112 and cysteine 187
Cysteine 138 and cysteine 142
Cysteine 138 and cysteine 219
Cysteine 287 and cysteine 324
Cysteine 142 and cysteine 219
Cysteine 323 and cysteine 324
Cysteine 287 and cysteine 323
Cysteine 287 and cysteine 287
Cysteine 219 and cysteine 528
6tpk A 112 A 187
A redox-regulated disulphide may form within Oxytocin receptor between cysteines 112 and 187.
Details
Redox score ?
85
PDB code
6tpk
Structure name
crystal structure of the human oxytocin receptor
Structure deposition date
2019-12-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P30559
Residue number A
112
Residue number B
187
Peptide name
Oxytocin receptor
Ligandability
Cysteine 112 of Oxytocin receptor
Cysteine 187 of Oxytocin receptor
6tpk A 138 A 142
A redox-regulated disulphide may form within Oxytocin receptor between cysteines 138 and 142.
Details
Redox score ?
72
PDB code
6tpk
Structure name
crystal structure of the human oxytocin receptor
Structure deposition date
2019-12-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
34
Peptide accession
P30559
Residue number A
138
Residue number B
142
Peptide name
Oxytocin receptor
Ligandability
Cysteine 138 of Oxytocin receptor
Cysteine 142 of Oxytocin receptor
6tpk A 138 A 219
A redox-regulated disulphide may form within Oxytocin receptor between cysteines 138 and 219.
Details
Redox score ?
67
PDB code
6tpk
Structure name
crystal structure of the human oxytocin receptor
Structure deposition date
2019-12-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
42
Peptide accession
P30559
Residue number A
138
Residue number B
219
Peptide name
Oxytocin receptor
Ligandability
Cysteine 138 of Oxytocin receptor
Cysteine 219 of Oxytocin receptor
6tpk A 287 A 324
A redox-regulated disulphide may form within Oxytocin receptor between cysteines 287 and 324. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
6tpk
Structure name
crystal structure of the human oxytocin receptor
Structure deposition date
2019-12-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
58
Peptide accession
P30559
Residue number A
287
Residue number B
324
Peptide name
Oxytocin receptor
Ligandability
Cysteine 287 of Oxytocin receptor
Cysteine 324 of Oxytocin receptor
6tpk A 142 A 219
A redox-regulated disulphide may form within Oxytocin receptor between cysteines 142 and 219. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6tpk
Structure name
crystal structure of the human oxytocin receptor
Structure deposition date
2019-12-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
38
Peptide accession
P30559
Residue number A
142
Residue number B
219
Peptide name
Oxytocin receptor
Ligandability
Cysteine 142 of Oxytocin receptor
Cysteine 219 of Oxytocin receptor
6tpk A 323 A 324
A redox-regulated disulphide may form within Oxytocin receptor between cysteines 323 and 324. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6tpk
Structure name
crystal structure of the human oxytocin receptor
Structure deposition date
2019-12-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
62
Peptide accession
P30559
Residue number A
323
Residue number B
324
Peptide name
Oxytocin receptor
Ligandability
Cysteine 323 of Oxytocin receptor
Cysteine 324 of Oxytocin receptor
6tpk A 287 A 323
A redox-regulated disulphide may form within Oxytocin receptor between cysteines 287 and 323. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6tpk
Structure name
crystal structure of the human oxytocin receptor
Structure deposition date
2019-12-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
66
Peptide accession
P30559
Residue number A
287
Residue number B
323
Peptide name
Oxytocin receptor
Ligandability
Cysteine 287 of Oxytocin receptor
Cysteine 323 of Oxytocin receptor
6tpk A 287 A 322
A redox-regulated disulphide may form within Oxytocin receptor between cysteines 287 and 287 (287 and 322 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
6tpk
Structure name
crystal structure of the human oxytocin receptor
Structure deposition date
2019-12-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
82
Peptide accession
P30559
Residue number A
287
Residue number B
287
Peptide name
Oxytocin receptor
Ligandability
Cysteine 287 of Oxytocin receptor
Cysteine 287 of Oxytocin receptor
Uncertain whether structure cysteine 322 has been assigned to correct residue.
6tpk A 473 A 528
A redox-regulated disulphide may form within Oxytocin receptor between cysteines 219 and 528 (473 and 528 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
6tpk
Structure name
crystal structure of the human oxytocin receptor
Structure deposition date
2019-12-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
84
Peptide accession
P30559
Residue number A
219
Residue number B
528
Peptide name
Oxytocin receptor
Ligandability
Cysteine 219 of Oxytocin receptor
Cysteine 528 of Oxytocin receptor
Cysteine 528 in protein B could not be asigned to a Uniprot residue.
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