ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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fMet-Leu-Phe receptor

Intermolecular
Cysteine 126 and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Intramolecular
Cysteine 98 and cysteine 176
Cysteine 124 and cysteine 126
Cysteine 253 and cysteine 295
A redox-regulated disulphide may form between cysteine 126 of fMet-Leu-Phe receptor 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 ?
59
PDB code
7vfx
Structure name
the structure of formyl peptide receptor 1 in complex with gi and peptide agonist fmifl
Structure deposition date
2021-09-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
90
Peptide A name
fMet-Leu-Phe receptor
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P21462
Peptide B accession
P63096
Peptide A residue number
126
Peptide B residue number
351

Ligandability

Cysteine 126 of fMet-Leu-Phe receptor

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 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1

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 fMet-Leu-Phe receptor between cysteines 98 and 176.

Details

Redox score ?
85
PDB code
7vfx
Structure name
the structure of formyl peptide receptor 1 in complex with gi and peptide agonist fmifl
Structure deposition date
2021-09-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P21462
Residue number A
98
Residue number B
176
Peptide name
fMet-Leu-Phe receptor

Ligandability

Cysteine 98 of fMet-Leu-Phe receptor

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 176 of fMet-Leu-Phe receptor

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 fMet-Leu-Phe receptor between cysteines 124 and 126. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7t6t
Structure name
molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors fpr1 and fpr2
Structure deposition date
2021-12-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
74
Peptide accession
P21462
Residue number A
124
Residue number B
126
Peptide name
fMet-Leu-Phe receptor

Ligandability

Cysteine 124 of fMet-Leu-Phe receptor

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 126 of fMet-Leu-Phe receptor

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 fMet-Leu-Phe receptor between cysteines 253 and 295. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7vfx
Structure name
the structure of formyl peptide receptor 1 in complex with gi and peptide agonist fmifl
Structure deposition date
2021-09-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
58
Peptide accession
P21462
Residue number A
253
Residue number B
295
Peptide name
fMet-Leu-Phe receptor

Ligandability

Cysteine 253 of fMet-Leu-Phe receptor

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 295 of fMet-Leu-Phe receptor

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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